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Yu, L.;  Qian, Z.;  Ge, J.;  Du, R. Structure and Properties of Glucansucrase. Encyclopedia. Available online: https://encyclopedia.pub/entry/36314 (accessed on 18 April 2024).
Yu L,  Qian Z,  Ge J,  Du R. Structure and Properties of Glucansucrase. Encyclopedia. Available at: https://encyclopedia.pub/entry/36314. Accessed April 18, 2024.
Yu, Liansheng, Zhigang Qian, Jingping Ge, Renpeng Du. "Structure and Properties of Glucansucrase" Encyclopedia, https://encyclopedia.pub/entry/36314 (accessed April 18, 2024).
Yu, L.,  Qian, Z.,  Ge, J., & Du, R. (2022, November 24). Structure and Properties of Glucansucrase. In Encyclopedia. https://encyclopedia.pub/entry/36314
Yu, Liansheng, et al. "Structure and Properties of Glucansucrase." Encyclopedia. Web. 24 November, 2022.
Structure and Properties of Glucansucrase
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This entry is adapted from the peer-reviewed paper 10.3390/fermentation8110629

Glucansucrase (GS) belongs to the GH70 family, which not only can synthesize exopolysaccharides (EPSs) with different physicochemical properties through glucosyl transglycosylation (by hydrolyzing sucrose) but can also produce oligosaccharides. 

lactic acid bacteria glucansucrase exopolysaccharides

1. Introduction

Polysaccharide polymers are one of the most valuable natural substances, and they play an important role in the fields of medical devices, food chemicals, and ecological and environmental protection [1]. Among them, the production of microbial exopolysaccharide (EPS) has the characteristics of being unaffected by environmental factors and easier downstream processing compared with plants, algae, fungi, and petroleum-based EPSs, which makes it shine in the field of production [2]. Bacterial enzymes involved in the production of EPS from sucrose, termed glucansucrases (GSs), are extracellular enzymes that can be assisted by branched sucrases (BRSs). GSs belong to the glycoside hydrolase GH70, which are very efficient transglycosylases and do not require expensive nucleotide-activated sugars (NDP-sugars) [3][4][5].
GSs are additionally named glucosyltransferases (GTFs), which catalyze the synthesis of EPSs and oligosaccharides using the glucose unit from the sucrose donor. GSs are applied in the fields of feed, food, medicine, and other engineering fields because of their outstanding physicochemical properties [6][7]. Bacterial GSs are mainly produced by lactic acid bacteria (LAB), a group of Gram-positive bacteria like Leuconostoc, Streptococcus, Lactobacillus, and Weissella species [8][9][10]. According to the glycosidic linkages present in the polymer, these enzymes are classified as (i) the synthesis of dextran by dextransucrases, consisting mainly of α-1,6 linkage and some α-1,2, α-1,3 and α-1,6 branches, (ii) the synthesis of mutan α-1,3, by mutansucrases (iii) forming alternan via alternansucrase, composed of alternating α-1,6 and α-1,3 glucosidic linkages, and (iv) reuteransucrase synthesizing reuteran containing α-1,4 and α-1,6 linkages [5]. These enzymes additionally catalyze the formation of oligosaccharide and glycoconjugate products in the presence of sucrose and nonsucrose receptor substrates [9][11][12].
EPSs and oligosaccharides are being extensively studied for their prospects toward probiotics by stimulating the growth of probiotic strains or beneficial endogenous strains from the gastrointestinal tract [13][14][15]. Although these investigations have touched on a few imperative issues, such as the approximate structure of GS, uncovering the relationship between the structure and activity of GS and its component of activity are still issues to be unraveled.

2. Structure of the GS

Sequence similarity analysis showed that GSs belonged to the GH70 family of glycoside hydrolases, with an average molecular weight of about 160 kDa and an optimum temperature and pH of 30 °C and 5.0–6.0, respectively [16][17]. GSs have been found from Lactobacillus kunkeei H3 and H25 have a mass of 300 kDa [18]. Due to the relatively large molecular weight of enzymes, and structural analysis being very difficult, only the crystal structures of four GSs have been resolved. However, with the advent of the cryoelectron microscopy technology revolution, it is possible to resolve protein structure using a high resolution, which will help to promote the 3D structure exploration and characterization of GS.
Amino acid sequence analysis showed that the GSs from LAB share a frequent structure and are composed of four different domains: (i) a sign peptide, followed by using (ii) an extraordinarily variable stretch, (iii) a quite conserved catalytic or sucrose-binding domain and (iv) a C-terminal glucan binding domain composed of a series of tandem repeats [16][19]. Currently, crystallographic analysis of the 3D structure of Lactobacillus GSs showed that they contain a common domain organization. A truncated enzyme was used for crystallization [5]. With the elucidation of the 3D structure of GTF180-∆N, the hypothesis of the ring arrangement was confirmed [20][21]. Different from the previous prediction of the primary structure of the enzyme, the three-dimensional structure of the truncated GSs formed five domains (domain A, domain B, domain C, domain IV, and domain V) and are arranged as C-A-B-IV-V lines (Figure 1). Except for domain C, these four domains are composed of two discontinuous polypeptide chains at the N-terminal and C-terminal ends. Among them, A, B, and C are catalytic cores, while IV and V are unique to GH70 GS [5]. The active site of the GSs is located at the interface of domain A and domain B [22], providing residues for the active site gap and their possible role in determining the ligation specificity of the product is discussed.

Fermentation 08 00629 g001

Figure 1. Schematic diagram of the 3D structure of GS. (a) Schematic representation of the U-shape fold formed by the various domains of GS. (b) Schematic diagram of the 3D structure of Ln. reuteri GTF-180N (PDB: 3HZ3) and sucrose binding site. Sucrose molecules are shown in red, residues in domain A are shown in green carbon, and residues in domain B are shown in yellow at the bottom right. (c) Schematic diagram of the 3D structure of Ln. mesenteroides NRRL B-1355 Asr (PDB: 6HVG) and Ca2+ binding sites. The green circles represent Ca2+.

Domain A consists of (β/α)8 barrels and contains a catalytic site with the catalytic residue at the bottom of the domain. A crystal structure analysis of the GTF180-N mutant D1025N bound to sucrose [23][24] confirmed that these three residues constitute the catalytic site of GS. Domain B can form a Ca2+ binding site in domain A, which are used to form the binding site of substrate and receptor [5]. Domain C is located at the U-shaped bottom end of GS. It is the only domain in GH70 GS enzymes that is formed by a continuous polypeptide segment, but its function is still unclear. IV and V are additional domains; the structure of domain IV is different from that of any other known protein and only occurs in GH70 enzymes (Figure 1) [5][24].
Domain V is adjacent to domain IV. It contains several repeats and has been shown to be involved in glucan binding [13] and is a glucan-binding domain that is involved, to a certain extent, in glucan extension and enzymatic processing, providing a high-affinity anchoring platform for the synthesis of high-molecular-weight dextran [25][26]. There may well be subtle interactions between the V domain and the catalytic domain. It can help capture the polymer chain and keep it near the active site to facilitate the extension or branching of the sugar chain. Partial or total truncation of domain V affects the binding capacity of glucan and also changes the size of the synthesized polymer. Structural analysis of domain V revealed the presence of a consensus β-solenoid fold with multiple copies [27]. In the crystal structure, it has a variety of conformations, mainly divided into two types, one is the extension to the active catalytic center, and the other is the extension to the outside of the conformation in Leuconostoc mesenteroides NRRL B-1355-alternating α-1,3/1,6-glucosyltransferase (Asr). Its domain V was found to extend to the catalytic core in Ln. reuteri GTF-180N. Its domain V was found to extend out of the conformation (Figure 1) [5][27].
The exact role of domain IV is unclear. It is speculated that domain IV acts as a hinge to promote the growth of glucan chains by directing the glucan chains bound to domain V towards or away from the catalytic site. The N-terminus of GS contains a signal peptide (36 to 40 amino acids) for its secretion [5][28]. The amino acid fragment between the signal peptide and the GS core region is highly variable in content and dimension (200 to 700 amino acids) [28]. The function of the N-terminal domain remains unknown.

3. Catalytic Mechanism of GS

Both the catalytic mechanism and structure of GH70 are closely related to the GH13 and GH77 families [24]. The newly discovered GH70 subfamily GtfB, GtfC, and GtfD are inactive against sucrose but can catalyze starch and maltodextrin to α-glucan [24]. The common characteristic of GH family enzymes is that they also use a catalytic (β/α)8 barrel domain to break down the α-glycosidic bonds between glucose and other glucose or fructose [29][30]. Robyt found there are two active sites; according to the GS catalytic reaction, one is composed of covalent β-glucose-enzyme intermediates under oxygen-carbon ion-like transformation conditions [5][31]. The β-glucose-enzyme intermediate is catalyzed through the a-retaining double displacement reaction, which involves three important residues: a nucleophile, an acid-base catalyst, and a transition state stabilizer (Figure 2). Aspartic acid, which first acts as a nucleophile, attacks the ectopic C1 carbon of the sucrose–glucose unit. Glutamate acts as an acid-base catalyst to transfer protons to fructose and release fructose. The transition state stabilizes the stable residue dimension and transitions to a covalent β-glucose-enzyme. Finally, the covalent β-glucosyl-enzyme is formed from the transition state stabilizer (Figure 2). The other is composed of chain and enzyme intermediates [30]. The C1 position in the later intermediate attacks the C6 position of the glucosyl group to form a glycosidic bond, thereby increasing the length [31]. Although the determinants of the size distribution of GS products have been broadly studied before, many are still unknown [26][32][33][34][35][36]. The N-terminal variable region and C-terminal glucan-binding domain have been indicated as playing a role in product size distribution [26].

Fermentation 08 00629 g002

Figure 2. General reaction mechanism for GH70 glucansucrases; D is the nucleophilic asparte residue; E is the general acid/base residue [27].
The catalytic mechanism of GS allows for the hydrolysis of sucrose to obtain a glucosyl-enzyme intermediate, and this mechanism is based on a detailed structural analysis of Bacillus circulans 251 CGTase [37]. Due to the different receptors, GS appears to synthesize different products: (i) through hydrolysis, water acts as a receptor and hydrolyses to glucose; (ii) through transglycosylation, the glucosyl moiety is converted to an accepting sugar after the fructose is discharged [27]. When substrate-only sucrose exists, GS hydrolyses sucrose to dextran; furthermore, due to the different amino acid sequences of the GS active center, the glycosidic bond composition and branching structure of the produced glucan is also different. Most of the synthesized glucans are composed of one or two types of glycosidic bonds, in which the composition ratio, branching degree, and branch length are also random, which depends on the amino acid sequences of the GS active center [38][39].

4. Isolation and Purification of GS

GS is an extracellular enzyme for which its structure and catalytic mechanism have not been clarified. In order to understand the structure and function of GS, it is necessary to isolate and purify GS [17]. Various GS purification methods, including salting-out and solvents [40], phase partition [41][42][43], polyethylene glycol fractioning [41][43][44], chromatography column [45][46][47], ultrafiltration [48], and combined processes such as sugaring and gel permeation chromatography [49][50].
Salting out, normally as ammonium sulfate precipitation, is when the ionic strength in a solution and the solubility of different proteins are different; high concentrations of salt ions compete with proteins for water molecules in protein solutions, therefore destroying the hydrated membrane on the surface of the protein, reducing its solubility, and allowing it to precipitate out of the solution. Due to different protein solubility, different concentrations of salt solution can be used to precipitate different proteins. Normally, people use ammonium sulfate precipitation as the first step for purification because of its high solubility. Robyt [51] thought ammonium sulfate would hurt the enzyme activity of GS as the concentration rose, especially to more than 80%.
At present, a variety of techniques have been successfully used for the isolation and purification of Ln. mesenteroides GS, and ultrafiltration and gel filtration chromatography are considered to be the best way to purify GS due to the resulting high recovery of enzyme activity. Miao [52] used freeze-drying ion-exchange chromatography and gel filtration methods to purify the enzyme. The crude enzyme solution was concentrated by freeze-drying and loaded into a DEAE-Sepharose FF 16/10 anion exchange column. Further purification was performed using Sepharose CL-6B gel filtration chromatography. The GS was purified 8.6-fold, and its specific activity was 1.3 IU/mg. Polyethylene glycol (PEG) is an uncharged linear macromolecular polymer, and its strong dehydration ability can destroy the hydration layer on the surface of protein molecules and cause protein precipitation. This method is cheap and easy to perform but it is easily affected by centrifugation temperature and pH, so it is usually used in combination with other methods. Song [16] precipitated the crude GS with 10% (v/v) PEG 2000 and then loaded it into a HiTrap Q FF anion exchange column and Sepharose CL-6B column. The purified fractions were dialyzed, concentrated, and collected, resulting in a specific activity of 1.4 U/mg protein, with 13.2-fold purification. Nigam et al. [53] compared the phase separation and purification effect of polyethylene glycol PEG 6000 and PEG 400 on dextransucrase, and the results showed that the tertiary phase separation effect of PEG 6000 was better; the final recovery rate was 84%, and the specific activity of the enzyme after purification.
The yield from GS separation by traditional separation technology is low, and its catalytic properties have not been thoroughly analyzed. In recent years, the cloning and expression of GS by means of genetic engineering is expected to overcome the shortcomings of low enzyme yield and expand the industrial application of the enzyme [54][55]. Kim et al. [56]. constructed Escherichia coli BL21 (DE3) carrying the Ln. lactis EG001 GS gene. The crude enzyme was mixed with Ni-NTA agarose, and the mixture was loaded onto a chromatography column. The proteins were eluted, and the specific activity of the purified enzyme showed an increase of over 2.3-fold with respect to the crude enzyme. Amari [54] et al. constructed engineered bacteria that could express the dextransucrase gene of W. confusa C39-2. The recombinant enzyme was purified using an affinity chromatography protocol, and the activity was 4-fold higher. At present, GS derived from a variety of LAB has been isolated and purified, and its structure and properties have been continuously analyzed (Table 1).
Table 1. Information on GS from different strains and their related properties in recent years was analyzed and collated using the CAZy database.
Enzyme MASS Organism Genebank Length Reference
Gtf1624 183 kDa Latilactobacillus curvatus TMW 1.624 CCK33643.1 1697 aa [57]
DSR-F 170 kDa Ln. citreum B/110-1-2 ACY92456.2 1527 aa [58]
LcDS 165 kDa Ln. citreum HJ-P4 BAF96719.1 1477 aa [59]
DexT 167 kDa Ln citreum KM20 ACA83218.1 1495 aa [60]
DSR-A 145 kDa Ln. citreum NRRL B-1299 CDX67012.1 1290 aa [61]
DSR-B 168 kDa Ln. citreum NRRL B-1299 AAB95453.1 1508 aa [62]
DSR-E 313 kDa Ln. citreum NRRL B-1299 CDX66820.1 2836 aa [63]
DSR-DP - Ln. citreum NRRL B-1299 CDX66641.1 1278 aa [63]
DSR-M 144 kDa Ln. citreum NRRL B-1299 CDX66895.1 1293 aa [61]
DexYG 170 kDa Ln. mesenteroides 0326 ABC75033.1 1527 aa [64]
DsrBCB4 168 kDa Ln. mesenteroides B-1299CB4 ABF85832.1 1505 aa [65]
DsrC 165 kDa Ln. mesenteroides B-1355 CAB76565.1 1477 aa [66]
Dsrb74 169 kDa Ln. mesenteroides B-742CB AAG38021.1 1508 aa [67]
DsrP 161 kDa Ln. mesenteroides IBT-PQ AAS79426.1 1454 aa [68]
DsrN 169 kDa Ln. mesenteroides KIBGE-IB-22 AFP53921.1 1527 aa [69]
DsrX 169 kDa Ln. mesenteroides L0309 AAQ98615.2 1522 aa [70]
DsrD 169 kDa Ln. mesenteroides LCC4 AAG61158.1 1527 aa [50]
DSR-S 169 kDa Ln. mesenteroides NRRL B-512F AAD10952.1 1527 aa [71]
DSR-T 110 kDa Ln. mesenteroides NRRL B-512F BAA90527.1 1016 aa [72]
Gtf1971 178 kDa Ligilactobacillus animalis TMW 1.971 CCK33644.1 1585 aa [57]
Gtf106A 199 kDa L. reuteri TMW 1.106 ABP88726.1 1782 aa [57]
GTF-S 151 kDa Streptococcus downei MFE 28 AAA26898.1 1365 aa [73]
GTF-U 176 kDa Streptococcus sobrinus BAA14241.1 1592 aa [74]
GTF-B 166 kDa Streptococcus mutans GS 5 AAA88588.1 1476 aa [75]
GTF-D 163 kDa S. mutans GS 5 AAA26895.1 1462 aa [76]
DsrK39 158 kDa Weissella cibaria LBAE-K39 ADB43097.3 1445 aa [77]
WcCab3-DSR 154 kDa Weissella confusa Cab3 AKE50934.1 1401 aa [78]
DSR-C39-2 155 kDa W. confusa LBAE C39-2 CCF30682.1 1412 aa [54]
DSR 156 kDa W. confusa VTT E-90392 AHU88292.1 1418 aa [79]
LcALT 229 kDa Ln. citreum ABK-1 AIM52834.1 2057 aa [80]
GtfB-SK2 - Ln. citreum SK24.002 - - [81]
ASR 229 kDa Ln. mesenteroides NRRL B-1355 CAB65910.2 2057 aa [82]
GtfO 197 kDa L. reuteri ATCC 55730 AAY86923.1 1781 aa [83]
Gtf-SK3 - L. reuteri SK24.003 - - [84]
GtfML1 - L. reuteri ML1 - - [34]
DSRI - Ln. mesenteroides NRRL B-1118 - - [85]
GtfB - S. mutans GS5 - - [86]
GtfC - S. mutans GS5 - - [87]
GTF-Kg15 174 kDa Latilactobacillus sakei KG15 AAU08011.1 1595 aa [34]
GTF-33 172 kDa Lentilactobacillus parabuchneri 33 AAU08006.1 1561 aa [34]
- 164 kDa Leuconostoc lactis EG001 ACT20911.1 1500 aa [56]
GTF-Kg3 161 kDa Limosilactobacillus fermentum KG3 AAU08008.1 1463 aa [34]
GtfB 179 kDa L. f ermentum NCC2970 AOR73699.1 1593 aa [88]
GtfB 179 kDa L. reuteri 121 AAU08014.2 1619 aa [89]
GtfML1 196 kDa L. reuteri ML1 AAU08004.1 1772 aa [34]
GtfML4 180 kDa L. reuteri ML1 AAU08003.2 1620 aa [90]
GtfB 196 kDa L. reuteri NCC2613 ASA47879.1 1662 aa [91]
GtfC 163 kDa S. mutans BAA26114.1 1455 aa [89]
DsrwC 162 kDa W. cibaria CMU ACK38203.1 1472 aa [92]
GtfD 87 kDa Azotobacter chroococcum NCIMB 8003 AJE22990.1 780 aa [93]
GtfC 99 kDa Exiguobacterium sibiricum 255-15 ACB62096.1 893 aa [94]

5. Physiological and Biochemical Properties of GS

Many factors can affect the catalytic activity of GS, including pH, temperature, and some organic solvents and metal ions. According to Kralj [34], the maximum GS activity from L. reuteri was gained at a pH of 4.0–5.5, which is comparable with most papers. Miao [52] found that GS from L. reuteri SK24.003 retained high activity at a low pH, showing better acid-resistance. However, a pH value that is too high or too low is still not conducive to the synthesis of GS. Previous studies have shown that GS has the highest purity and the most stable activity at pH 7 [95], while a low pH can significantly reduce enzyme synthesis. The analysis of the GS produced by Ln. mesenteroides DRP2-19 and isolated from sauerkraut showed that the optimum pH for GS was 5.56, and the synthesis of GS was severely affected at pH < 4.5 or >7, which corroborated the previous point [96]. Because of the different sources and structures of GSs, the optimum reaction temperature for each GS is different. Generally, the optimum range is from 30–40°C in culture. When the temperature exceeds 45 °C, the enzyme activity begins to decrease, and when it exceeds 50 °C, the enzyme loss is more obvious. Most double-charged ions (Mg2+, Mn2+, Ni2+, Co2+, Ca2+, Fe2+, and Zn2+) activated enzyme activity, suggesting it was a metal-activated enzyme [52]. GS has a calcium ion activation site, which can increase enzyme activity. It is concluded that calcium ion can enhance the activity of dextransucrase. The stability of the entire edifice is enhanced by calcium coordination, which likely reinforces the interaction between the two domains [97]. Qader et al. [98] found that when the concentration of CaCl2 was 0.005%, the enzyme activity increased to 108.26 DSU/mL/h, which was 2.03 times higher than that of the control group. When the content of CaCl2 was higher than 0.005%, enzyme activity decreased gradually. Some reports found that when Ca2+ is within a certain concentration range, Ca2+ will preferentially bind to the activation site on the enzyme, and the activation effect is stronger than the inhibitory effect. Furthermore, Hg+, Zn2+, Cu2+, Pb2+, and Fe3+ had a strong inhibitory effect on enzyme activity, which was the same as in previous reports; when copper ions were present, there was no transferase activity [99]. The activity and stability of GS in the presence of organic solvents were related to the solvent concentration and its nature. Chemical inhibitors indicate that the function of amino acid residues is located at the GS-active site [16]. Most chemical inhibitors had an inhibition effect on GS, like sodium dodecyl sulfate (SDS), ethylene diamine, tetraacetic acid (EDTA), and β-Mercaptoethanol (β-ME) [25][100]. Other chemical reagents, including butanol, n-hexane, chloroform, calcium ammonium nitrate (CAN), and ethyl acetate, also inhibited the activity of GS with increasing concentrations, whereas glycerol, formaldehyde, and dimethyl sulfoxide (DMSO) enhanced the activity of GS to a certain extent [101].

References

  1. Xu, Y.; Cui, Y.; Yue, F.; Liu, L.; Shan, Y.; Liu, B.; Zhou, Y.; Lü, X. Exopolysaccharides produced by lactic acid bacteria and Bifidobacteria: Structures, physiochemical functions and applications in the food industry. Food Hydrocoll. 2019, 94, 475–499.
  2. Rana, S.; Upadhyay, L.S.B. Microbial exopolysaccharides: Synthesis pathways, types and their commercial applications. Int. J. Biol. Macromol. 2020, 157, 577–583.
  3. Pham, H.; Pijning, T.; Dijkhuizen, L.; van Leeuwen, S.S. Mutational analysis of the role of the glucansucrase Gtf180-ΔN active site residues in product and linkage specificity with lactose as acceptor substrate. J. Agric. Food Chem. 2018, 66, 12544–12554.
  4. Meng, X.; Pijning, T.; Tietema, M.; Dobruchowska, J.M.; Yin, H.; Gerwig, G.J.; Kralj, S.; Dijkhuizen, L. Characterization of the glucansucrase GTF180 W1065 mutant enzymes producing polysaccharides and oligosaccharides with altered linkage composition. Food Chem. 2017, 217, 81–90.
  5. Molina, M.; Cioci, G.; Moulis, C.; Séverac, E.; Remaud-Siméon, M. Bacterial α-glucan and branching sucrases from GH70 family: Discovery, structure–function relationship studies and engineering. Microorganisms 2021, 9, 1607.
  6. Holt, S.M.; Skory, C.; Cote, G. Enzymatic synthesis of artificial polysaccharides. ACS Sustain. Chem. Eng. 2020, 8, 11853–11871.
  7. Chen, Z.; Ni, D.; Zhang, W.; Stressler, T.; Mu, W. Lactic acid bacteria-derived α-glucans: From enzymatic synthesis to miscellaneous applications. Biotechnol. Adv. 2021, 47, 107708.
  8. Kim, M.; Jang, J.-K.; Park, Y.-S. Production optimization, structural analysis, and prebiotic-and anti-inflammatory effects of gluco-oligosaccharides produced by Leuconostoc lactis SBC001. Microorganisms 2021, 9, 200.
  9. Hasselwander, O.; DiCosimo, R.; You, Z.; Cheng, Q.; Rothman, S.C.; Suwannakham, S.; Baer, Z.C.; Roesch, B.M.; Ruebling-Jass, K.D.; Lai, J.P. Development of dietary soluble fibres by enzymatic synthesis and assessment of their digestibility in vitro, animal and randomised clinical trial models. Int. J. Food Sci. Nutr. 2017, 68, 849–864.
  10. Saadat, Y.R.; Khosroushahi, A.Y.; Gargari, B.P. A comprehensive review of anticancer, immunomodulatory and health beneficial effects of the lactic acid bacteria exopolysaccharides. Carbohydr. Polym. 2019, 217, 79–89.
  11. Sarbini, S.R.; Kolida, S.; Naeye, T.; Einerhand, A.W.; Gibson, G.R.; Rastall, R.A. The prebiotic effect of α-1, 2 branched, low molecular weight dextran in the batch and continuous faecal fermentation system. J. Funct. Foods 2013, 5, 1938–1946.
  12. Sarbini, S.R.; Kolida, S.; Naeye, T.; Einerhand, A.; Brison, Y.; Remaud-Simeon, M.; Monsan, P.; Gibson, G.R.; Rastall, R.A. In vitro fermentation of linear and α-1, 2-branched dextrans by the human fecal microbiota. Appl. Environ. Microbiol. 2011, 77, 5307–5315.
  13. Daba, G.M.; Elnahas, M.O.; Elkhateeb, W.A. Contributions of exopolysaccharides from lactic acid bacteria as biotechnological tools in food, pharmaceutical, and medical applications. Int. J. Biol. Macromol. 2021, 173, 79–89.
  14. Korcz, E.; Kerényi, Z.; Varga, L. Dietary fibers, prebiotics, and exopolysaccharides produced by lactic acid bacteria: Potential health benefits with special regard to cholesterol-lowering effects. Food Funct. 2018, 9, 3057–3068.
  15. Kabli, M.; İspirli, H.; Balubaid, M.; Taylan, O.; Yılmaz, M.T.; Dertli, E. Optimization of lactose derivative hetero-oligosaccharides production using whey as the acceptor molecule by an active glucansucrase. Biocatal. Biotransform. 2022, 40, 9–16.
  16. Song, L.; Miao, M.; Jiang, B.; Xu, T.; Cui, S.W.; Zhang, T. Leuconostoc citreum SK24.002 glucansucrase: Biochemical characterisation and de novo synthesis of α-glucan. Int. J. Biol. Macromol. 2016, 91, 123–131.
  17. Guzman, G.Y.F.; Hurtado, G.B.; Ospina, S.A. New dextransucrase purification process of the enzyme produced by Leuconostoc mesenteroides IBUN 91.2. 98 based on binding product and dextranase hydrolysis. J. Biotechnol. 2018, 265, 8–14.
  18. Vasileva, T.; Bivolarski, V.; Michailova, G.; Salim, A.; Rabadjiev, Y.; Ivanova, I.; Iliev, I. Glucansucrases produced by fructophilic lactic acid bacteria Lactobacillus kunkeei H3 and H25 isolated from honeybees. J. Basic Microbiol. 2017, 57, 68–77.
  19. Meng, X.; Li, X.; Pijning, T.; Wang, X.; van Leeuwen, S.S.; Dijkhuizen, L.; Chen, G.; Liu, W. Characterization of the (engineered) branching sucrase gtfz-cd2 from Apilactobacillus kunkeei for efficient glucosylation of benzenediol compounds. Appl. Environ. Microbiol. 2022, 88, e01031-22.
  20. Vujičić-Žagar, A.; Pijning, T.; Kralj, S.; López, C.A.; Eeuwema, W.; Dijkhuizen, L.; Dijkstra, B.W. Crystal structure of a 117 kDa glucansucrase fragment provides insight into evolution and product specificity of GH70 enzymes. Proc. Natl. Acad. Sci. USA 2010, 107, 21406–21411.
  21. Ito, K.; Ito, S.; Shimamura, T.; Weyand, S.; Kawarasaki, Y.; Misaka, T.; Abe, K.; Kobayashi, T.; Cameron, A.D.; Iwata, S. Crystal structure of glucansucrase from the dental caries pathogen Streptococcus mutans. J. Mol. Biol. 2011, 408, 177–186.
  22. Stam, M.R.; Danchin, E.G.; Rancurel, C.; Coutinho, P.M.; Henrissat, B. Dividing the large glycoside hydrolase family 13 into subfamilies: Towards improved functional annotations of α-amylase-related proteins. Protein Eng. Des. Sel. 2006, 19, 555–562.
  23. Gangoiti, J.; Pijning, T.; Dijkhuizen, L. Biotechnological potential of novel glycoside hydrolase family 70 enzymes synthesizing α-glucans from starch and sucrose. Biotechnol. Adv. 2018, 36, 196–207.
  24. Meng, X.; Gangoiti, J.; Bai, Y.; Pijning, T.; Van Leeuwen, S.S.; Dijkhuizen, L. Structure–function relationships of family GH70 glucansucrase and 4, 6-α-glucanotransferase enzymes, and their evolutionary relationships with family GH13 enzymes. Cell. Mol. Life Sci. 2016, 73, 2681–2706.
  25. Wu, D.T.; Zhang, H.B.; Huang, L.J.; Hu, X.Q. Purification and characterization of extracellular dextranase from a novel producer, Hypocrea lixii F1002, and its use in oligodextran production. Process Biochem. 2011, 46, 1942–1950.
  26. Moulis, C.; Vaca Medina, G.; Suwannarangsee, S.; Monsan, P.; Remaud-Simeon, M.; Potocki-Veronese, G. One-step synthesis of isomalto-oligosaccharide syrups and dextrans of controlled size using engineered dextransucrase. Biocatal. Biotransform. 2008, 26, 141–151.
  27. Leemhuis, H.; Pijning, T.; Dobruchowska, J.M.; van Leeuwen, S.S.; Kralj, S.; Dijkstra, B.W.; Dijkhuizen, L. Glucansucrases: Three-dimensional structures, reactions, mechanism, α-glucan analysis and their implications in biotechnology and food applications. J. Biotechnol. 2013, 163, 250–272.
  28. van Hijum, S.A.; Kralj, S.; Ozimek, L.K.; Dijkhuizen, L.; van Geel-Schutten, I.G. Structure-function relationships of glucansucrase and fructansucrase enzymes from lactic acid bacteria. Microbiol. Mol. Biol. Rev. 2006, 70, 157–176.
  29. André, I.; Potocki-Véronese, G.; Morel, S.; Monsan, P.; Remaud-Siméon, M. Sucrose-utilizing transglucosidases for biocatalysis. Carbohydr. Sustain. Dev. I 2010, 294, 25–48.
  30. Korakli, M.; Vogel, R.F. Structure/function relationship of homopolysaccharide producing glycansucrases and therapeutic potential of their synthesised glycans. Appl. Microbiol. Biotechnol. 2006, 71, 790–803.
  31. Robyt, J.F.; Yoon, S.H.; Mukerjea, R. Dextransucrase and the mechanism for dextran biosynthesis. Carbohydr. Res. 2008, 343, 3039–3048.
  32. Falconer, D.J.; Mukerjea, R.; Robyt, J.F. Biosynthesis of dextrans with different molecular weights by selecting the concentration of Leuconostoc mesenteroides B-512FMC dextransucrase, the sucrose concentration, and the temperature. Carbohydr. Res. 2011, 346, 280–284.
  33. Kim, D.; Robyt, J.F.; Lee, S.Y.; Lee, J.H.; Kim, Y.M. Dextran molecular size and degree of branching as a function of sucrose concentration, pH, and temperature of reaction of Leuconostoc mesenteroides B-512FMCM dextransucrase. Carbohydr. Res. 2003, 338, 1183–1189.
  34. Kralj, S.; van Geel-Schutten, G.H.; Dondorff, M.M.G.; Kirsanovs, S.; Van Der Maarel, M.; Dijkhuizen, L. Glucan synthesis in the genus Lactobacillus: Isolation and characterization of glucansucrase genes, enzymes and glucan products from six different strains. Microbiology 2004, 150, 3681–3690.
  35. Lee, M.S.; Cho, S.K.; Eom, H.J.; Kim, S.Y.; Kim, T.J.; Han, N.S. Optimized substrate concentrations for production of long-chain isomaltooligosaccharides using dextransucrase of Leuconostoc mesenteroides B-512F. J. Microbiol. Biotechnol. 2008, 18, 1141–1145.
  36. Meng, X.; Dobruchowska, J.M.; Pijning, T.; Gerwig, G.J.; Kamerling, J.P.; Dijkhuizen, L. Truncation of domain V of the multidomain glucansucrase GTF180 of Lactobacillus reuteri 180 heavily impairs its polysaccharide-synthesizing ability. Appl. Microbiol. Biotechnol. 2015, 99, 5885–5894.
  37. Lawson, C.L.; van Montfort, R.; Strokopytov, B.; Rozeboom, H.J.; Kalk, K.H.; de Vries, G.E.; Penninga, D.; Dijkhuizen, L.; Dijkstra, B.W. Nucleotide sequence and X-ray structure of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 in a maltose-dependent crystal form. J. Mol. Biol. 1994, 236, 590–600.
  38. Kralj, S.; Eeuwema, W.; Eckhardt, T.H.; Dijkhuizen, L. Role of asparagine 1134 in glucosidic bond and transglycosylation specificity of reuteransucrase from Lactobacillus reuteri 121. FEBS J. 2006, 273, 3735–3742.
  39. van Leeuwen, S.S.; Kralj, S.; van Geel-Schutten, I.H.; Gerwig, G.J.; Dijkhuizen, L.; Kamerling, J.P. Structural analysis of the α-D-glucan (EPS180) produced by the Lactobacillus reuteri strain 180 glucansucrase GTF180 enzyme. Carbohydr. Res. 2008, 343, 1237–1250.
  40. Rodrigues, S.; Lona, L.; Franco, T. Effect of phosphate concentration on the production of dextransucrase by Leuconostoc mesenteroides NRRL B512F. Bioprocess Biosyst. Eng. 2003, 26, 57–62.
  41. Otts, D.; Day, D.F. Dextransucrase secretion in Leuconostoc mesenteroides depends on the presence of a transmembrane proton gradient. J. Bacteriol. 1988, 170, 5006–5011.
  42. Quirasco, M.; Lopez-Munguia, A.; Remaud-Simeon, M.; Monsan, P.; Farres, A. Induction and transcription studies of the dextransucrase gene in Leuconostoc mesenteroides NRRL B-512F. Appl. Environ. Microbiol. 1999, 65, 5504–5509.
  43. Goyal, A.; Katiyar, S.S. Fractionation of Leuconostoc mesenteroides NRRL B-512F dextran sucrase by polyethylene glycol: A simple and effective method purification. J. Microbiol. Methods 1994, 20, 225–231.
  44. Purama, R.K.; Goyal, A. Identification, effective purification and functional characterization of dextransucrase from Leuconostoc mesenteroides NRRL B-640. Bioresour. Technol. 2008, 99, 3635–3642.
  45. Kobayashi, M.; Matsuda, K. Electrophoretic analysis of the multiple forms of dextransucrase from Leuconostoc mesenteroides. J. Biochem. 1986, 100, 615–621.
  46. Miller, A.W.; Eklund, S.H.; Robyt, J.F. Milligram to gram scale purification and characterization of dextransucrase from Leuconostoc mesenteroides NRRL B-512F. Carbohydr. Res. 1986, 147, 119–133.
  47. Miller, A.W.; Robyt, J.F. Stabilization of dextransucrase from Leuconostoc mesenteroides NRRL B-512F by nonionic detergents, poly(ethylene glycol) and high-molecular-weight dextran. Biochim. Biophys. Acta (BBA)-Protein Struct. Mol. Enzymol. 1984, 785, 89–96.
  48. Kitaoka, M.; Robyt, J.F. Use of a microtiter plate screening method for obtaining Leuconostoc mesenteroides mutants constitutive for glucansucrase. Enzym. Microb. Technol. 1998, 22, 527–531.
  49. Monsan, P.; Lopez, A. On the production of dextran by free and immobilized dextransucrase. Biotechnol. Bioeng. 1981, 23, 2027–2037.
  50. Neubauer, H.; Bauche, A.; Mollet, B. Molecular characterization and expression analysis of the dextransucrase DsrD of Leuconostoc mesenteroides Lcc4 in homologous and heterologous Lactococcus lactis cultures. Microbiology 2003, 149, 973–982.
  51. Robyt, J.F.; Walseth, T.F. Production, purification, and properties of dextransucrase from Leuconostoc mesenteroides NRRL B-512F. Carbohydr. Res. 1979, 68, 95–111.
  52. Miao, M.; Ma, Y.; Jiang, B.; Cui, S.W.; Jin, Z.; Zhang, T. Characterisations of Lactobacillus reuteri SK24. 003 glucansucrase: Implications for α-gluco-poly and oligosaccharides biosynthesis. Food Chem. 2017, 222, 105–112.
  53. Nigam, M.; Goyal, A.; Katiyar, S.S. High yield purification of dextransucrase from Leuconostoc mesenteroides NRRL B-512F by phase partitioning. J. Food Biochem. 2006, 30, 12–20.
  54. Amari, M.; Arango, L.; Gabriel, V.; Robert, H.; Morel, S.; Moulis, C.; Gabriel, B.; Remaud-Siméon, M.; Fontagné-Faucher, C. Characterization of a novel dextransucrase from Weissella confusa isolated from sourdough. Appl. Microbiol. Biotechnol. 2013, 97, 5413–5422.
  55. Wang, C.; Chen, S.; Zhang, H.B.; Li, Y.; Hu, X.Q. Characterization of the inserted mutagenesis dextransucrases from Leuconostoc mesenteroides 0326 to produce hyperbranched dextran. Int. J. Biol. Macromol. 2018, 112, 584–590.
  56. Kim, Y.M.; Yeon, M.J.; Choi, N.S.; Chang, Y.H.; Jung, M.Y.; Song, J.J.; Kim, J.S. Purification and characterization of a novel glucansucrase from Leuconostoc lactis EG001. Microbiol. Res. 2010, 165, 384–391.
  57. Rühmkorf, C.; Bork, C.; Mischnick, P.; Rübsam, H.; Becker, T.; Vogel, R.F. Identification of Lactobacillus curvatus TMW 1.624 dextransucrase and comparative characterization with Lactobacillus reuteri TMW 1.106 and Lactobacillus animalis TMW 1.971 dextransucrases. Food Microbiol. 2013, 34, 52–61.
  58. Vidal, R.F.; Martínez, A.; Moulis, C.; Escalier, P.; Morel, S.; Remaud-Simeon, M.; Monsan, P. A novel dextransucrase is produced by Leuconostoc citreum strain B/110-1-2: An isolate used for the industrial production of dextran and dextran derivatives. J. Ind. Microbiol. Biotechnol. 2011, 38, 1499–1506.
  59. Yi, A.R.; Lee, S.R.; Jang, M.U.; Park, J.M.; Eom, H.J.; Han, N.S.; Kim, T.J. Cloning of dextransucrase gene from Leuconostoc citreum HJ-P4 and its high-level expression in E. coli by low temperature induction. J. Microbiol. Biotechnol. 2009, 19, 829–835.
  60. Ko, J.A.; Jeong, H.J.; Ryu, Y.B.; Park, S.J.; Wee, Y.J.; Kim, D.; Kim, Y.M.; Lee, W.S. Large increase in Leuconostoc citreum KM20 dextransucrase activity achieved by changing the strain/inducer combination in an E. coli expression system. J. Microbiol. Biotechnol. 2012, 22, 510–515.
  61. Passerini, D.; Vuillemin, M.; Ufarté, L.; Morel, S.; Loux, V.; Fontagné-Faucher, C.; Monsan, P.; Remaud-Siméon, M.; Moulis, C. Inventory of the GH70 enzymes encoded by Leuconostoc citreum NRRL B-1299-identification of three novel α-transglucosylases. FEBS J. 2015, 282, 2115–2130.
  62. Monchois, V.; Remaud-Simeon, M.; Monsan, P.; Willemot, R.M. Cloning and sequencing of a gene coding for an extracellular dextransucrase (DSRB) from Leuconostoc mesenteroides NRRL B-1299 synthesizing only a alpha (1-6) glucan. FEMS Microbiol. Lett. 1998, 159, 307–315.
  63. Bozonnet, S.; Dols-Laffargue, M.; Fabre, E.; Pizzut, S.; Remaud-Simeon, M.; Monsan, P.; Willemot, R.M. Molecular characterization of DSR-E, an alpha-1,2 linkage-synthesizing dextransucrase with two catalytic domains. J. Bacteriol. 2002, 184, 5753–5761.
  64. Zhang, H.; Hu, Y.; Zhu, C.; Zhu, B.; Wang, Y. Cloning, sequencing and expression of a dextransucrase gene (dexYG) from Leuconostoc mesenteroides. Biotechnol. Lett. 2008, 30, 1441–1446.
  65. Kang, H.K.; Kim, Y.M.; Kim, D.M. Functional, genetic, and bioinformatic characterization of dextransucrase (DSRBCB4) gene in Leuconostoc mesenteroides B-1299 CB4. J. Microbiol. Biotechnol. 2008, 18, 1050–1058.
  66. Yoon, S.H.; Fulton, D.B.; Robyt, J.F. Enzymatic synthesis of L-DOPA alpha-glycosides by reaction with sucrose catalyzed by four different glucansucrases from four strains of Leuconostoc mesenteroides. Carbohydr. Res. 2010, 345, 1730–1735.
  67. Yoon, S.H.; Bruce Fulton, D.; Robyt, J.F. Enzymatic synthesis of two salicin analogues by reaction of salicyl alcohol with Bacillus macerans cyclomaltodextrin glucanyltransferase and Leuconostoc mesenteroides B-742CB dextransucrase. Carbohydr. Res. 2004, 339, 1517–1529.
  68. Chellapandian, M.; Larios, C.; Sanchez-Gonzalez, M.; Lopez-Munguia, A. Production and properties of a dextransucrase from Leuconostoc mesenteroides IBT-PQ isolated from ‘pulque’, a traditional Aztec alcoholic beverage. J. Ind. Microbiol. Biotechnol. 1998, 21, 51–56.
  69. Siddiqui, N.N.; Aman, A.; Qader, S.A. Mutational analysis and characterization of dextran synthesizing enzyme from wild and mutant strain of Leuconostoc mesenteroides. Carbohydr. Polym. 2013, 91, 209–216.
  70. Yalin, Y.; Jin, L.; Jianhua, W.; Da, T.; Zigang, T. Expression and characterization of dextransucrase gene dsrX from Leuconostoc mesenteroides in Escherichia coli. J. Biotechnol. 2008, 133, 505–512.
  71. Monchois, V.; Remaud-Simeon, M.; Russell, R.R.; Monsan, P.; Willemot, R.M. Characterization of Leuconostoc mesenteroides NRRL B-512F dextransucrase (DSRS) and identification of amino-acid residues playing a key role in enzyme activity. Appl. Microbiol. Biotechnol. 1997, 48, 465–472.
  72. Funane, K.; Ishii, T.; Matsushita, M.; Hori, K.; Mizuno, K.; Takahara, H.; Kitamura, Y.; Kobayashi, M. Water-soluble and water-insoluble glucans produced by Escherichia coli recombinant dextransucrases from Leuconostoc mesenteroides NRRL B-512F. Carbohydr. Res. 2001, 334, 19–25.
  73. Gilmore, K.S.; Russell, R.R.; Ferretti, J.J. Analysis of the Streptococcus downei gtfS gene, which specifies a glucosyltransferase that synthesizes soluble glucans. Infect. Immun. 1990, 58, 2452–2458.
  74. Hanada, N.; Fukushima, K.; Nomura, Y.; Senpuku, H.; Hayakawa, M.; Mukasa, H.; Shiroza, T.; Abiko, Y. Cloning and nucleotide sequence analysis of the Streptococcus sobrinus gtfU gene that produces a highly branched water-soluble glucan. Biochim. Biophys. Acta 2002, 1570, 75–79.
  75. Tsumori, H.; Minami, T.; Kuramitsu, H.K. Identification of essential amino acids in the Streptococcus mutans glucosyltransferases. J. Bacteriol. 1997, 179, 3391–3396.
  76. Shimamura, A.; Nakano, Y.J.; Mukasa, H.; Kuramitsu, H.K. Identification of amino acid residues in Streptococcus mutans glucosyltransferases influencing the structure of the glucan product. J. Bacteriol. 1994, 176, 4845–4850.
  77. Bounaix, M.S.; Robert, H.; Gabriel, V.; Morel, S.; Remaud-Siméon, M.; Gabriel, B.; Fontagné-Faucher, C. Characterization of dextran-producing Weissella strains isolated from sourdoughs and evidence of constitutive dextransucrase expression. FEMS Microbiol. Lett. 2010, 311, 18–26.
  78. Shukla, S.; Shi, Q.; Maina, N.H.; Juvonen, M.; Goyal, A. Weissella confusa Cab3 dextransucrase: Properties and in vitro synthesis of dextran and glucooligosaccharides. Carbohydr. Polym. 2014, 101, 554–564.
  79. Kajala, I.; Shi, Q.; Nyyssölä, A.; Maina, N.H.; Hou, Y.; Katina, K.; Tenkanen, M.; Juvonen, R. Cloning and characterization of a Weissella confusa dextransucrase and its application in high fibre baking. PLoS ONE 2015, 10, e0116418.
  80. Wangpaiboon, K.; Padungros, P.; Nakapong, S.; Charoenwongpaiboon, T.; Rejzek, M.; Field, R.A.; Pichyangkura, R. An α-1,6-and α-1,3-linked glucan produced by Leuconostoc citreum ABK-1 alternansucrase with nanoparticle and film-forming properties. Sci. Rep. 2018, 8, 8340.
  81. Miao, M.; Ma, Y.; Jiang, B.; Huang, C.; Li, X.; Cui, S.W.; Zhang, T. Structural investigation of a neutral extracellular glucan from Lactobacillus reuteri SK24.003. Carbohydr. Polym. 2014, 106, 384–392.
  82. Argüello-Morales, M.A.; Remaud-Simeon, M.; Pizzut, S.; Sarçabal, P.; Willemot, R.; Monsan, P. Sequence analysis of the gene encoding alternansucrase, a sucrose glucosyltransferase from Leuconostoc mesenteroides NRRL B-1355. FEMS Microbiol. Lett. 2000, 182, 81–85.
  83. Kralj, S.; Stripling, E.; Sanders, P.; van Geel-Schutten, G.H.; Dijkhuizen, L. Highly hydrolytic reuteransucrase from probiotic Lactobacillus reuteri strain ATCC 55730. Appl. Environ. Microbiol. 2005, 71, 3942–3950.
  84. Miao, M.; Ma, Y.; Huang, C.; Jiang, B.; Cui, S.W.; Zhang, T. Physicochemical properties of a water soluble extracellular homopolysaccharide from Lactobacillus reuteri SK24.003. Carbohydr. Polym. 2015, 131, 377–383.
  85. Côté, G.L.; Skory, C.D. Cloning, expression, and characterization of an insoluble glucan-producing glucansucrase from Leuconostoc mesenteroides NRRL B-1118. Appl. Microbiol. Biotechnol. 2012, 93, 2387–2394.
  86. Shiroza, T.; Ueda, S.; Kuramitsu, H.K. Sequence analysis of the gtfB gene from Streptococcus mutans. J. Bacteriol. 1987, 169, 4263–4270.
  87. Ueda, S.; Shiroza, T.; Kuramitsu, H.K. Sequence analysis of the gtfC gene from Streptococcus mutans GS-5. Gene 1988, 69, 101–109.
  88. Gangoiti, J.; van Leeuwen, S.S.; Gerwig, G.J.; Duboux, S.; Vafiadi, C.; Pijning, T.; Dijkhuizen, L. 4,3-α-Glucanotransferase, a novel reaction specificity in glycoside hydrolase family 70 and clan GH-H. Sci. Rep. 2017, 7, 39761.
  89. Dobruchowska, J.M.; Gerwig, G.J.; Kralj, S.; Grijpstra, P.; Leemhuis, H.; Dijkhuizen, L.; Kamerling, J.P. Structural characterization of linear isomalto-/malto-oligomer products synthesized by the novel GTFB 4,6-α-glucanotransferase enzyme from Lactobacillus reuteri 121. Glycobiology 2012, 22, 517–528.
  90. Leemhuis, H.; Dijkman, W.P.; Dobruchowska, J.M.; Pijning, T.; Grijpstra, P.; Kralj, S.; Kamerling, J.P.; Dijkhuizen, L. 4,6-α-Glucanotransferase activity occurs more widespread in Lactobacillus strains and constitutes a separate GH70 subfamily. Appl. Microbiol. Biotechnol. 2013, 97, 181–193.
  91. Pijning, T.; Gangoiti, J.; Te Poele, E.M.; Börner, T.; Dijkhuizen, L. Insights into Broad-Specificity Starch Modification from the Crystal Structure of Limosilactobacillus Reuteri NCC 2613 4,6-α-Glucanotransferase GtfB. J. Agric. Food Chem. 2021, 69, 13235–13245.
  92. Kang, H.K.; Oh, J.S.; Kim, D. Molecular characterization and expression analysis of the glucansucrase DSRWC from Weissella cibaria synthesizing a alpha (1→6) glucan. FEMS Microbiol. Lett. 2009, 292, 33–41.
  93. Gangoiti, J.; van Leeuwen, S.S.; Vafiadi, C.; Dijkhuizen, L. The Gram-negative bacterium Azotobacter chroococcum NCIMB 8003 employs a new glycoside hydrolase family 70 4,6-α-glucanotransferase enzyme (GtfD) to synthesize a reuteran like polymer from maltodextrins and starch. Biochim. Biophys. Acta 2016, 1860, 1224–1236.
  94. Gangoiti, J.; Pijning, T.; Dijkhuizen, L. The Exiguobacterium sibiricum 255-15 GtfC Enzyme Represents a Novel Glycoside Hydrolase 70 Subfamily of 4,6-α-Glucanotransferase Enzymes. Appl. Environ. Microbiol. 2016, 82, 756–766.
  95. Tsuchiya, H.; Koepsell, H.; Corman, J.; Bryant, G.; Bogard, M.; Feger, V.; Jackson, R. The effect of certain cultural factors on production of dextransucrase by Leuconostoc mesenteroides. J. Bacteriol. 1952, 64, 521–526.
  96. Du, R.; Zhao, F.; Pan, L.; Han, Y.; Xiao, H.; Zhou, Z. Optimization and purification of glucansucrase produced by Leuconostoc mesenteroides DRP2-19 isolated from Chinese Sauerkraut. Prep. Biochem. Biotechnol. 2018, 48, 465–473.
  97. Molina, M.; Moulis, C.; Monties, N.; Pizzut-Serin, S.; Guieysse, D.; Morel, S.; Cioci, G.; Remaud-Simeéon, M. Deciphering an undecided enzyme: Investigations of the structural determinants involved in the linkage specificity of alternansucrase. ACS Catal. 2019, 9, 2222–2237.
  98. Qader, S.A.U.; Aman, A.; Bano, S.; Syed, N.; Azhar, A. The effect of calcium ions and temperature on the production, activity and stability of dextransucrase from the newly isolated strain Leuconostoc mesenteroides PCSIR-4. Rom. J. Biochem. 2008, 45, 159–168.
  99. Bai, Y.; van der Kaaij, R.M.; Leemhuis, H.; Pijning, T.; van Leeuwen, S.S.; Jin, Z.; Dijkhuizen, L. Biochemical characterization of the Lactobacillus reuteri glycoside hydrolase family 70 GTFB type of 4, 6-α-glucanotransferase enzymes that synthesize soluble dietary starch fibers. Appl. Environ. Microbiol. 2015, 81, 7223–7232.
  100. Côté, G.L.; Robyt, J.F. Isolation and partial characterization of an extracellular glucansucrase from Leuconostoc mesenteroides NRRL B-1355 that synthesizes an alternating (1→6), (1→3)-α-D-glucan. Carbohydr. Res. 1982, 101, 57–74.
  101. Du, R.; Qiao, X.; Wang, Y.; Zhao, B.; Han, Y.; Zhou, Z. Determination of glucansucrase encoding gene in Leuconostoc mesenteroides. Int. J. Biol. Macromol. 2019, 137, 761–766.
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Subjects: Biotechnology & Applied Microbiology
Contributors MDPI registered users' name will be linked to their SciProfiles pages. To register with us, please refer to https://encyclopedia.pub/register :
Liansheng Yu
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Zhigang Qian
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Jingping Ge
,
Renpeng Du
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Update Date: 25 Nov 2022
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