Submitted Successfully!
To reward your contribution, here is a gift for you: A free trial for our video production service.
Thank you for your contribution! You can also upload a video entry or images related to this topic.
Version Summary Created by Modification Content Size Created at Operation
1 -- 1442 2023-03-20 10:12:11 |
2 format correct + 4 word(s) 1446 2023-03-21 06:40:51 |

Video Upload Options

Do you have a full video?

Confirm

Are you sure to Delete?
Cite
If you have any further questions, please contact Encyclopedia Editorial Office.
Kamilari, E.; Stanton, C.; Reen, F.J.; Ross, R.P.; Kamilari, E. Production of Enzymes with Industrial Interest. Encyclopedia. Available online: https://encyclopedia.pub/entry/42344 (accessed on 28 March 2024).
Kamilari E, Stanton C, Reen FJ, Ross RP, Kamilari E. Production of Enzymes with Industrial Interest. Encyclopedia. Available at: https://encyclopedia.pub/entry/42344. Accessed March 28, 2024.
Kamilari, Eleni, Catherine Stanton, F. Jerry Reen, R. Paul Ross, Elena Kamilari. "Production of Enzymes with Industrial Interest" Encyclopedia, https://encyclopedia.pub/entry/42344 (accessed March 28, 2024).
Kamilari, E., Stanton, C., Reen, F.J., Ross, R.P., & Kamilari, E. (2023, March 20). Production of Enzymes with Industrial Interest. In Encyclopedia. https://encyclopedia.pub/entry/42344
Kamilari, Eleni, et al. "Production of Enzymes with Industrial Interest." Encyclopedia. Web. 20 March, 2023.
Production of Enzymes with Industrial Interest
Edit

Industrial enzymes are enzymes that are commercially used in a variety of industries such as pharmaceuticals, chemical production, biofuels, food & beverage, and consumer products.  

Geotrichum candidum yeast fungi lipases cellulases antimicrobial compounds proteases pectinases

1. Lytic Polysaccharide Monooxygenases (LPMOs)

Increasing demands of transportation fuel consumption (i.e., oil and biofuels), have prompted industries to invest in potentially renewable sources of energy production, such as plant biomass [1]. The main components of plant cell walls are cellulose, some non-cellulosic polysaccharides, and lignin. Plant biomass-derived lignocellulosic residues are considered great sources of fermentable sugars, the processing of which may lead to the production of renewable liquid transport fuels [2][3][4][5]. Morel and coworkers [6] identified the presence of genes encoding lignocellulolytic enzymes in the genome of G. candidum strain CLIB 918 (ATCC 204307). These enzymes included lytic polysaccharide monooxygenases (LPMOs) of the AA9 family, GH45 endoglucanases, which are strong oxidative enzymes that are important for the degradation of cellulose and hemicelluloses, such as xyloglucan and glucomannan [7], and endo-polygalacturonases. Similarly, G. candidum 3C was found to encode functional lytic LPMOs of the AA9 family [8][9]. LPMOs produced by G. candidum are promising candidates for enzymatic cocktails applied in biorefineries enrichment. Moreover, a cellulase isolated from G. candidum GAD1 was found to be promising for the degradation of carboxymethylcellulose salt from agricultural waste (rice straw), the fermentation of which resulted in bioethanol production [10].
Due to their improved catalytic activity against cellulose and hemicelluloses, some G. candidum strains were used for filter paper and cotton degradation. For instance, G. candidum strain 3C was discovered to encode a glycoside hydrolase (GH) of the family 7 cellobiohydrolases (CBHs), named Cel7A [11]. This strain’s cellulase complex exhibited more effective activity than that of Hypocrea jecorina, the most commonly used species for cellulase production [12]. An enzymatic cocktail from G. candidum strain 3C named ‘Cellokandin G10x’ has been applied for industrial pulp and wastepaper utilization [11]. Similarly, enzymatic isolates from G. candidum strain Dec 1 were found to improve kraft pulp bleaching [13]. Noteworthy, ITS, 18S rDNA, 28S rDNA, and RPB2 gene sequence comparisons and multiple sequencing analysis of G. candidum strain 3C indicated that the strain should be included within the genus Scytalidium (Pezizomycotina, Leotiomycetes) and renamed Scytalidium candidum 3C comb. nov. [14].

2. Lipases

G. candidum can produce extracellular lipases, especially when cultured in the presence of an inducer, such as triglycerides or olive oil, in the culture medium [15][16][17][18][19]. Lipases have numerous industrial applications, including the manufacture of enantiomerically pure pharmaceuticals, cosmetics, agrochemicals, surfactants, biolubricants, construction and destruction of biopolymers, waste-water-treatment, influence on food products’ sensorial characteristics, detergent industries, etc. [20][21][22][23]. Ferreira and coworkers [24] used a lipase secreted by G. candidum (GCL-I) to produce free fatty acids from olive, palm kernel, and cottonseed oils. Glycerol and free fatty acids are used by oleochemical industries to produce several products, including personal care products, such as shampoos, coatings, adhesives, surfactants, fatty alcohols, and lubricating oils [25][26][27]. G. candidum (ATCC 34614) was found to produce four lipases with different substrate specificities [28]. Specifically, lipases I and II indicated non-regional specificity with triolein, while lipases III and IV catalyzed the hydrolysis of triolein oleoyl esters at the sn-2 position with greater specificity compared to the sn-1(3) position, indicating an sn-2-regioselectivity. Laguerre and coworkers [29] indicated that the lipases isolated from G. candidum NRRL Y-552 were able to hydrolyze triolein and six edible oils, producing high amounts of diacylglycerol (DAG)-1,3 and lower amounts of DAG-1,2(2,3). The reduction in DAG-1,3 in oils with increased DAG-1,3 concentration is of great importance for the production of foods containing nutraceutical diacylglycerols able to reduce the levels of triacylglycerol in the plasma. Moreover, G. candidum lipase (LGC-I) was administered to produce decyl oleate ester from rice husks (phenyl-silica), which were chemically modified [30]. Furthermore, GCL-I and -II were applied for the hydrolysis or ethanolysis of Crambe and Camelina oils, producing high concentrations of erucic acid and gondoic acid [31].
To be applied as a biocatalyst, the lipases produced during fermentation by G. candidum need to be immobilized. Ferreira and coworkers [32] analyzed different approaches for purified lipase immobilization, to reveal that the most efficient protocol was ionic adsorption on MANAE-agarose. The molecular masses of the currently identified and purified lipases produced by Geotrichum sp. range from 32 kDa to 75 kDa [21][33][34][35][36][37][38]. Moreover, administration of endo-β-N-acetylglucosaminidase showed that these lipases are glycosylated, and beyond their high homology, they have different substrate specificity [39]. Furthermore, chemically modified to contain more amino groups, surface lipase produced by G. candidum (GCL) indicated faster and easiest immobilization on carboxymethyl and sulfopropyl agarose-based supports [39][40]. Administration of the ionic derivatives into fish oil resulted in increased hydrolysis and production of a high yield of Omega-3 polyunsaturated fatty acids (6.65 U and 7.85 U per gram of support of carboxymethyl derivative and sulfopropyl derivative, respectively) [39].

3. Alkaline Proteases

Investigation into the production of proteases from 30 G. candidum strains revealed that the proteolytic activity differs among the different strains [41]. More recently, 12 strains were tested for their ability to secrete proteases, from which one strain, G. candidum GCQAU01 isolated from the fermented milk product Dahiwas, was found to produce an ideal protease for industrial application [42]. Specifically, the identified serine-type protease indicated thermostability, had stable activity at temperatures ranging from 25 to 45 °C and pH 8–9, possessed increased hydrolytic activity against casein and bovine serum albumin (BSA), and its activity was prevented by PMSF (7.5%). Alkaline proteases are of great biotechnological importance due to their numerous applications in food, pharmaceutical and tannery industries, silver recovery, detergents and waste treatment, and amino acid resolution [43].

4. Pectinases

Pectinases produced by Geotrichum spp., such as G. candidum AA15, are considered good candidates to be applied by the fruit juice industry for clarification of juices [44][45]. The presence of pectin and several other components of fruits makes the produced juice cloudy [46], degrading its qualitative characteristics and affecting consumers’ preferences. Additionally, increased levels of pectin lead to an unwanted colloid texture formation [46]. The application of filtration can reduce the presence of pectin [47]. However, the increased presence of fiber-like molecules in pectin’s structure makes filtration inefficient for eliminating its existence in juice. Therefore, the addition of pectinolytic enzymes before the filtration process has been applied for the depectinization of several juices [48]. As a result, the process efficiency is increased [49]. The majority of pectinases are isolated from filamentous fungi, including Aspergillus niger [50]. However, the administration of pectinases from yeasts, such as Geotrichum, offers the advantages that: (a) some species are considered as generally recognized as safe (GRAS) [51]; (b) they produce an efficient type of pectinase for juice clarification [45]; and (c) they produce considerable amounts of pectinases in a shorter fermentation period compared to filamentous fungi [52]. Ahmed and Sohail [44] applied a response surface approach to reveal that the pectinase isolated from G. candidum AA15 was efficient for orange juice clarification, with the highest enzymatic activity in incubation time of 25 min at 35 °C, in pH 5. To increase the G. candidum AA15 pectinase yield, the strain was immobilized using corncob [45]. Additionally, simple sugars, such as xylose, galacturonic acid, galactose, and pectin, but not glucose, positively affected pectinase production in immobilized yeast cells [53].

5. Aldehyde Dehydrogenases, Glutamate Dehydrogenases, and Baeyer–Villiger Monooxygenases

Several enzymes associated with oxidation reactions have been applied by pharmaceutical and chemical industries for the oxidation of alcohols, sulfides, aldehydes, Baeyer–Villiger oxidation, and hydroxylation [54][55][56][57][58][59]. G. candidum was discovered to produce dehydrogenases with broad applications in organic synthesis [57][60][61][62][63][64][65][66]. For instance, G. candidum NBRC 4597 (GcAPRD) was discovered to produce a novel alcohol dehydrogenase (ALDH), acetophenone reductase, an enzyme with broad spectrum activity regarding the oxidation of aldehydes to carboxylic acids and selective activity for the oxidation of dialdehydes to aldehydic acids [61][67][68]. This process has important agrochemical and pharmaceutical applications, but there are still limitations on its use due to its limited recyclability [69]. The specific ALDH was found to have broad-spectrum activity, thermostability, and resistance to non-aqueous solvents [65][66][70][71][72][73]. The application of an organic–inorganic nanocrystal formation method successfully immobilized the isolated GcALDH nanocrystal, which retained its enzymatic activity and proved more thermostable compared to the free GcALDH [74]. The same team used graphene oxide and reduced graphene oxide, which are chemically produced oxidized forms of graphene, to immobilize GcAPRD, enabling its recycling [75]. As a result, a great number of ketones, such as the aliphatic ketone 3-hexanone, were decreased with 99% efficacy.
G. candidum S12 was shown to produce a novel glutamate dehydrogenase, which was highly active against glutamate, hexanol, α-ketoglutarate, and isoamyl alcohol (Km values of 41.74, 4.01, 20.37, and 19.37 mM, respectively) [76]. The catalytic activity against hexanol was enhanced by the addition of ADP, K+, Fe2+, and Zn2+ and reduced by EDTA, Mn2+, Pb2+, ATP, and DTT.
Furthermore, immobilization of the whole G. candidum CCT 1205 cell on functionalized silica resulted in ε-caprolactone creation, an advanced polymer with several biomedical applications [77]. E-caprolactone was also produced by whole G. candidum CCT 1205 cells using cyclohexenone, cyclohexanone, and cyclohexanol as substrates [78].

References

  1. Tan, H.-T.; Corbin, K.R.; Fincher, G.B. Emerging technologies for the production of renewable liquid transport fuels from biomass sources enriched in Plant cell walls. Front. Plant Sci. 2016, 7, 1854.
  2. Naik, S.N.N.; Goud, V.V.; Rout, P.K.; Dalai, A.K. Production of first and second generation biofuels: A comprehensive review. Renew. Sustain. Energy Rev. 2010, 14, 578–597.
  3. Cherubini, F. The biorefinery concept: Using biomass instead of oil for producing energy and chemicals. Energy Convers. Manag. 2010, 51, 1412–1421.
  4. Tilman, D.; Hill, J.; Lehman, C. Carbon-negative biofuels from low-input high-diversity grassland biomass. Science 2006, 314, 1598–1600.
  5. Hill, J.; Nelson, E.; Tilman, D.; Polasky, S.; Tiffany, D. Environmental, economic, and energetic costs and benefits of biodiesel and ethanol biofuels. Proc. Natl. Acad. Sci. USA 2006, 103, 11206–11210.
  6. Morel, G.; Sterck, L.; Swennen, D.; Marcet-Houben, M.; Onesime, D.; Levasseur, A.; Jacques, N.; Mallet, S.; Couloux, A.; Labadie, K.; et al. Differential gene retention as an evolutionary mechanism to generate biodiversity and adaptation in yeasts. Sci. Rep. 2015, 5, 11571.
  7. Berrin, J.-G.; Rosso, M.-N.; Hachem, M.A. Fungal secretomics to probe the biological functions of lytic polysaccharide monooxygenases. Carbohydr. Res. 2017, 448, 155–160.
  8. Ladevèze, S.; Haon, M.; Villares, A.; Cathala, B.; Grisel, S.; Herpoël-Gimbert, I.; Henrissat, B.; Berrin, J.-G. The yeast Geotrichum candidum encodes functional lytic polysaccharide monooxygenases. Biotechnol. Biofuels 2017, 10, 215.
  9. Valinhas, R.V.; Pantoja, L.A.; Maia, A.C.F.; Miguel, M.G.C.; Vanzela, A.P.F.; Nelson, D.L.; Santos, A.S. Xylose fermentation to ethanol by new Galactomyces geotrichum and Candida akabanensis strains. PeerJ 2018, 6, e4673.
  10. Gad, A.M.; Suleiman, W.B.; El-Sheikh, H.H.; Elmezayen, H.A.; Beltagy, E.A. Characterization of Cellulase from Geotrichum candidum Strain Gad1 Approaching Bioethanol Production. Arab. J. Sci. Eng. 2022, 47, 6837–6850.
  11. Borisova, A.S.; Eneyskaya, E.V.; Bobrov, K.S.; Jana, S.; Logachev, A.; Polev, D.E.; Lapidus, A.L.; Ibatullin, F.M.; Saleem, U.; Sandgren, M.; et al. Sequencing, biochemical characterization, crystal structure and molecular dynamics of cellobiohydrolase Cel7A from Geotrichum candidum 3C. FEBS J. 2015, 282, 4515–4537.
  12. Cherry, J.R.; Fidantsef, A.L. Directed evolution of industrial enzymes: An update. Curr. Opin. Biotechnol. 2003, 14, 438–443.
  13. Shintani, N.; Shoda, M. Decolorization of oxygen-delignified bleaching effluent and biobleaching of oxygen-delignified kraft pulp by non-white-rot fungus Geotrichum candidum Dec 1. J. Environ. Sci. 2013, 25, S164–S168.
  14. Pavlov, I.Y.; Bobrov, K.S.; Sumacheva, A.D.; Masharsky, A.E.; Polev, D.E.; Zhurishkina, E.V.; Kulminskaya, A.A. Scytalidium candidum 3C is a new name for the Geotrichum candidum Link 3C strain. J. Basic Microbiol. 2018, 58, 883–891.
  15. Shimada, Y.; Sugihara, A.; Nagao, T.; Tominaga, Y. Induction of Geotrichum candidum lipase by long-chain fatty acids. J. Ferment. Bioeng. 1992, 74, 77–80.
  16. Ramos, E.Z.; Júnior, R.H.M.; de Castro, P.F.; Tardioli, P.W.; Mendes, A.A.; Fernandéz-Lafuente, R.; Hirata, D.B. Production and immobilization of Geotrichum candidum lipase via physical adsorption on eco-friendly support: Characterization of the catalytic properties in hydrolysis and esterification reactions. J. Mol. Catal. B Enzym. 2015, 118, 43–51.
  17. Asses, N.; Ayed, L.; Bouallagui, H.; Ben Rejeb, I.; Gargouri, M.; Hamdi, M. Use of Geotrichum candidum for olive mill wastewater treatment in submerged and static culture. Bioresour. Technol. 2009, 100, 2182–2188.
  18. Brabcová, J.; Zarevúcka, M.; Macková, M. Differences in hydrolytic abilities of two crude lipases from Geotrichum candidum 4013. Yeast 2010, 27, 1029–1038.
  19. Maldonado, R.R.; Burkert, J.F.M.; Mazutti, M.A.; Maugeri, F.; Rodrigues, M.I. Evaluation of lipase production by Geotrichum candidum in shaken flasks and bench-scale stirred bioreactor using different impellers. Biocatal. Agric. Biotechnol. 2012, 1, 147–151.
  20. Nicoletti, G.; Cipolatti, E.; Valerio, A.; Carbonera, N.G.; Soares, N.S.; Theilacker, E.; Ninow, J.L.; Oliveira, D. Evaluation of different methods for immobilization of Candida antarctica lipase B (CalB lipase) in polyurethane foam and its application in the production of geranyl propionate. Bioprocess Biosyst. Eng. 2015, 38, 1739–1748.
  21. Brabcová, J.; Demianová, Z.; Vondrášek, J.; Jágr, M.; Zarevúcka, M.; Palomo, J.M. Highly selective purification of three lipases from Geotrichum candidum 4013 and their characterization and biotechnological applications. J. Mol. Catal. B Enzym. 2013, 98, 62–72.
  22. Adlercreutz, P. Immobilisation and application of lipases in organic media. Chem. Soc. Rev. 2013, 42, 6406–6436.
  23. Hasan, F.; Shah, A.A.; Hameed, A. Industrial applications of microbial lipases. Enzym. Microb. Technol. 2006, 39, 235–251.
  24. Ferreira, M.M.; de Oliveira, G.F.; Basso, R.C.; Mendes, A.A.; Hirata, D.B. Optimization of free fatty acid production by enzymatic hydrolysis of vegetable oils using a non-commercial lipase from Geotrichum candidum. Bioprocess Biosyst. Eng. 2019, 42, 1647–1659.
  25. Santos, K.C.; Cassimiro, D.M.J.; Avelar, M.H.M.; Hirata, D.B.; de Castro, H.F.; Fernández-Lafuente, R.; Mendes, A.A. Characterization of the catalytic properties of lipases from plant seeds for the production of concentrated fatty acids from different vegetable oils. Ind. Crops Prod. 2013, 49, 462–470.
  26. Fraile, J.M.; García, J.I.; Herrerías, C.I.; Pires, E. Synthetic Transformations for the Valorization of Fatty Acid Derivatives. Synthesis 2017, 49, 1444–1460.
  27. Murty, V.R.; Bhat, J.; Muniswaran, P.K.A. Hydrolysis of oils by using immobilized lipase enzyme: A review. Biotechnol. Bioprocess Eng. 2002, 7, 57–66.
  28. Sugihara, A.; Shimada, Y.; Nakamura, M.; Nagao, T.; Tominaga, Y. Positional and fatty acid specificities of Geottichum candidum Upases. Protein Eng. Des. Sel. 1994, 7, 585–588.
  29. Laguerre, M.; Nlandu Mputu, M.; Brïys, B.; Lopez, M.; Villeneuve, P.; Dubreucq, E. Regioselectivity and fatty acid specificity of crude lipase extracts from Pseudozyma tsukubaensis, Geotrichum candidum, and Candida rugosa. Eur. J. Lipid Sci. Technol. 2017, 119, 1600302.
  30. Santos, L.F.S.; Silva, M.R.L.; Ferreira, E.E.A.; Gama, R.S.; Carvalho, A.K.F.; Barboza, J.C.S.; Luiz, J.H.H.; Mendes, A.A.; Hirata, D.B. Decyl oleate production by enzymatic esterification using Geotrichum candidum lipase immobilized on a support prepared from rice husk. Biocatal. Agric. Biotechnol. 2021, 36, 102142.
  31. Oroz-Guinea, I.; Zorn, K.; Bornscheuer, U.T. Enrichment of Erucic and Gondoic Fatty Acids from Crambe and Camelina Oils Catalyzed by Geotrichum candidum Lipases I and II. J. Am. Oil Chem. Soc. 2019, 96, 1327–1335.
  32. Ferreira, M.M.; Santiago, F.L.B.; da Silva, N.A.G.; Luiz, J.H.H.; Fernandéz-Lafuente, R.; Mendes, A.A.; Hirata, D.B. Different strategies to immobilize lipase from Geotrichum candidum: Kinetic and thermodynamic studies. Process Biochem. 2018, 67, 55–63.
  33. Bertolini, M.C.; Laramee, L.; Thomas, D.Y.; Cygler, M.; Schrag, J.D.; Vernet, T. Polymorphism in the lipase genes of Geotrichum candidum strains. JBIC J. Biol. Inorg. Chem. 1994, 219, 119–125.
  34. Shimada, Y.; Sugihara, A.; Iizumi, T.; Tominaga, Y. CDNA cloning and characterization of Geotrichum candidum lipase II. J. Biochem. 1990, 107, 703–707.
  35. Sugihara, A.; Shimada, Y.; Tominaga, Y. Separation and characterization of two molecular forms of Geotrichum candidum lipase. J. Biochem. 1990, 107, 426–430.
  36. Shimada, Y.; Sugihara, A.; Tominaga, Y.; Iizumi, T.; Tsunasawa, S.; Iizurni, T.; Susumu, T. CDNA molecular cloning of Geotrichum candidum lipase. J. Biochem. 1989, 106, 383–388.
  37. Gopinath, S.C.B.; Hilda, A.; Priya, T.L.; Annadurai, G.; Anbu, P. Purification of lipase from Geotrichum candidum: Conditions optimized for enzyme production using Box–Behnken design. World J. Microbiol. Biotechnol. 2003, 19, 681–689.
  38. Sidebottom, C.M.; Charton, E.; Dunn, P.P.J.; Mycock, G.; Davies, C.; Sutton, J.L.; Macrae, A.R.; Slabas, A.R. Geotrichum candidum produces several lipases with markedly different substrate specificities. JBIC J. Biol. Inorg. Chem. 1991, 202, 485–491.
  39. de Morais Júnior, W.G.; Terrasan, C.R.F.; Fernández-Lorente, G.; Guisán, J.M.; Ribeiro, E.J.; de Resende, M.M.; Pessela, B.C. Solid-phase amination of Geotrichum candidum lipase: Ionic immobilization, stabilization and fish oil hydrolysis for the production of Omega-3 polyunsaturated fatty acids. Eur. Food Res. Technol. 2017, 243, 1375–1384.
  40. de Morais Júnior, W.G.; Maia, A.M.; Martins, P.A.; Fernández-Lorente, G.; Guisán, J.M.; Pessela, B.C. Influence of different immobilization techniques to improve the enantioselectivity of lipase from Geotrichum candidum applied on the resolution of mandelic acid. Mol. Catal. 2018, 458, 89–96.
  41. Guéguen, M.; Lenoir, J. Aptitude de l’espèce Geotrichum candidum à la production d’enzymes protéolytiques. Le Lait 1975, 55, 145–162.
  42. Muhammad, A.; Imran, B.S.A.; Jean-Paul, V.; Muhammad, I.A.; Faryal, R.; Nathalie, D.; Muhammad, I. Purification, Characterization and thermodynamic assessment of an alkaline protease by Geotrichum candidum of dairy origin. Iran. J. Biotechnol. 2019, 17, 30–37.
  43. Agrawal, D.; Patidar, P.; Banerjee, T.; Patil, S. Production of alkaline protease by Penicillium sp. under SSF conditions and its application to soy protein hydrolysis. Process Biochem. 2004, 39, 977–981.
  44. Ahmed, A.; Sohail, M. Characterization of pectinase from Geotrichum candidum AA15 and its potential application in orange juice clarification. J. King Saud Univ.-Sci. 2020, 32, 955–961.
  45. Ejaz, U.; Ahmed, A.; Sohail, M. Statistical optimization of immobilization of yeast cells on corncob for pectinase production. Biocatal. Agric. Biotechnol. 2018, 14, 450–456.
  46. Vaillant, F.; Millan, P.; O’Brien, G.; Dornier, M.; Decloux, M.; Reynes, M. Crossflow microfiltration of passion fruit juice after partial enzymatic liquefaction. J. Food Eng. 1999, 42, 215–224.
  47. Sulaiman, M.Z.; Sulaiman, N.M.; Yih, L.S. Limiting permeate flux in the clarification of untreated starfruit juice by membrane ultrafiltration. Chem. Eng. J. 1998, 69, 145–148.
  48. Patidar, M.K.; Nighojkar, S.; Kumar, A.; Nighojkar, A. Pectinolytic enzymes-solid state fermentation, assay methods and applications in fruit juice industries: A review. 3 Biotech 2018, 8, 199.
  49. Rao, M.A.; Acree, T.E.; Cooley, H.J.; Ennis, R.W. Clarification of Apple Juice by Hollow Fiber Ultrafiltration: Fluxes and Retention of Odor-Active Volatiles. J. Food Sci. 1987, 52, 375–377.
  50. dos Santos, T.C.; dos Santos Reis, N.; Silva, T.P.; Machado, F.D.P.P.; Bonomo, R.C.F.; Franco, M. Prickly palm cactus husk as a raw material for production of ligninolytic enzymes by Aspergillus niger. Food Sci. Biotechnol. 2016, 25, 205–211.
  51. Lessa, O.A.; Reis, N.D.S.; Leite, S.G.F.; Gutarra, M.L.E.; Souza, A.O.; Gualberto, S.A.; de Oliveira, J.R.; Aguiar-Oliveira, E.; Franco, M. Effect of the solid state fermentation of cocoa shell on the secondary metabolites, antioxidant activity, and fatty acids. Food Sci. Biotechnol. 2017, 27, 107–113.
  52. Padma, P.N.; Anuradha, K.; Reddy, G. Pectinolytic yeast isolates for cold-active polygalacturonase production. Innov. Food Sci. Emerg. Technol. 2011, 12, 178–181.
  53. Ahmed, A.; Ejaz, U.; Sohail, M. Pectinase production from immobilized and free cells of Geotrichum candidum AA15 in galacturonic acid and sugars containing medium. J. King Saud Univ.-Sci. 2020, 32, 952–954.
  54. Hollmann, F.; Arends, I.W.C.E.; Buehler, K.; Schallmey, A.; Bühler, B. Enzyme-mediated oxidations for the chemist. Green Chem. 2011, 13, 226–265.
  55. Romano, D.; Villa, R.; Molinari, F. Preparative Biotransformations: Oxidation of Alcohols. Chemcatchem 2012, 4, 739–749.
  56. Ceccoli, R.D.; Bianchi, D.A.; Rial, D.V. Flavoprotein monooxygenases for oxidative biocatalysis: Recombinant expression in microbial hosts and applications. Front. Microbiol. 2014, 5, 25.
  57. Nakamura, K.; Inoue, Y.; Matsuda, T.; Misawa, I. Stereoselective oxidation and reduction by immobilized Geotrichum candidum in an organic solvent. J. Chem. Soc. Perkin Trans. 1 1999, 2397–2402.
  58. Mitsukura, K.; Sato, Y.; Yoshida, T.; Nagasawa, T. Oxidation of heterocyclic and aromatic aldehydes to the corresponding carboxylic acids by Acetobacter and Serratia strains. Biotechnol. Lett. 2004, 26, 1643–1648.
  59. Zhang, X.-Y.; Zong, M.-H.; Li, N. Whole-cell biocatalytic selective oxidation of 5-hydroxymethylfurfural to 5-hydroxymethyl-2-furancarboxylic acid. Green Chem. 2017, 19, 4544–4551.
  60. Koesoema, A.A.; Standley, D.M.; Senda, T.; Matsuda, T. Impact and relevance of alcohol dehydrogenase enantioselectivities on biotechnological applications. Appl. Microbiol. Biotechnol. 2020, 104, 2897–2909.
  61. Koesoema, A.A.; Standley, D.M.; Ohshima, S.; Tamura, M.; Matsuda, T. Control of enantioselectivity in the enzymatic reduction of halogenated acetophenone analogs by substituent positions and sizes. Tetrahedron Lett. 2020, 61, 151820.
  62. Koesoema, A.A.; Standley, D.M.; Sriwong, K.T.; Tamura, M.; Matsuda, T. Access to both enantiomers of substituted 2-tetralol analogs by a highly enantioselective reductase. Tetrahedron Lett. 2020, 61, 151682.
  63. Koesoema, A.A.; Sugiyama, Y.; Sriwong, K.T.; Xu, Z.; Verina, S.; Standley, D.M.; Senda, M.; Senda, T.; Matsuda, T. Reversible control of enantioselectivity by the length of ketone substituent in biocatalytic reduction. Appl. Microbiol. Biotechnol. 2019, 103, 9529–9541.
  64. Nakamura, K.; Matsuda, T. Asymmetric Reduction of Ketones by the Acetone Powder of Geotrichum candidum. J. Org. Chem. 1998, 63, 8957–8964.
  65. Matsuda, T.; Yamagishi, Y.; Koguchi, S.; Iwai, N.; Kitazume, T. An effective method to use ionic liquids as reaction media for asymmetric reduction by Geotrichum candidum. Tetrahedron Lett. 2006, 47, 4619–4622.
  66. Yamamoto, T.; Nakata, Y.; Cao, C.; Sugiyama, Y.; Asanuma, Y.; Kanamaru, S.; Matsuda, T. Acetophenone reductase with extreme stability against a high concentration of organic compounds or an elevated temperature. Appl. Microbiol. Biotechnol. 2013, 97, 10413–10421.
  67. Nakata, Y.; Fukae, T.; Kanamori, R.; Kanamaru, S.; Matsuda, T. Purification and characterization of acetophenone reductase with excellent enantioselectivity from Geotrichum candidum NBRC 4597. Appl. Microbiol. Biotechnol. 2009, 86, 625–631.
  68. Hoshino, T.; Yamabe, E.; Hawari, M.A.; Tamura, M.; Kanamaru, S.; Yoshida, K.; Koesoema, A.A.; Matsuda, T. Oxidation of aromatic and aliphatic aldehydes to carboxylic acids by Geotrichum candidum aldehyde dehydrogenase. Tetrahedron 2020, 76, 131387.
  69. Basso, A.; Serban, S. Industrial applications of immobilized enzymes—A review. Mol. Catal. 2019, 479, 110607.
  70. Matsuda, T.; Marukado, R.; Mukouyama, M.; Harada, T.; Nakamura, K. Asymmetric reduction of ketones by Geotrichum candidum: Immobilization and application to reactions using supercritical carbon dioxide. Tetrahedron Asymmetry 2008, 19, 2272–2275.
  71. Matsuda, T.; Watanabe, K.; Kamitanaka, T.; Harada, T.; Nakamura, K. Biocatalytic reduction of ketones by a semi-continuous flow process using supercritical carbon dioxide. Chem. Commun. 2003, 1198–1199.
  72. Matsuda, T.; Harada, T.; Nakamura, K. Alcohol dehydrogenase is active in supercritical carbon dioxide. Chem. Commun. 2000, 1367–1368.
  73. Koesoema, A.A.; Sugiyama, Y.; Xu, Z.; Standley, D.M.; Senda, M.; Senda, T.; Matsuda, T. Structural basis for a highly (S)-enantioselective reductase towards aliphatic ketones with only one carbon difference between side chain. Appl. Microbiol. Biotechnol. 2019, 103, 9543–9553.
  74. Sriwong, K.T.; Ogura, K.; Hawari, M.A.; Matsuda, T. Geotrichum candidum aldehyde dehydrogenase-inorganic nanocrystal with enhanced activity. Enzym. Microb. Technol. 2021, 150, 109866.
  75. Sriwong, K.T.; Kamogawa, R.; Issasi, C.S.C.; Sasaki, M.; Matsuda, T. Geotrichum candidum acetophenone reductase immobilization on reduced graphene oxide: A promising biocatalyst for green asymmetric reduction of ketones. Biochem. Eng. J. 2022, 177, 108263.
  76. Zhu, J.; Lu, K.; Xu, X.; Wang, X.; Shi, J. Purification and characterization of a novel glutamate dehydrogenase from Geotrichum candidum with higher alcohol and amino acid activity. AMB Express 2017, 7, 1–13.
  77. Silva, A.L.P.; Caridade, T.N.D.S.; Magalhães, R.R.; De Sousa, K.T.; De Sousa, C.C.; Vale, J.A. Biocatalytic production of Ɛ-caprolactone using Geotrichum candidum cells immobilized on functionalized silica. Appl. Microbiol. Biotechnol. 2020, 104, 8887–8895.
  78. Silva, A.L.P.; Batista, P.K.; Filho, A.D.; Junior, C.S.D.N.; Rebouças, J.S.; Vale, J.A. Rapid conversion of cyclohexenone, cyclohexanone and cyclohexanol to ε-caprolactone by whole cells of Geotrichum candidum CCT 1205. Biocatal. Biotransform. 2017, 35, 185–190.
More
Information
Contributors MDPI registered users' name will be linked to their SciProfiles pages. To register with us, please refer to https://encyclopedia.pub/register : , , , ,
View Times: 244
Revisions: 2 times (View History)
Update Date: 21 Mar 2023
1000/1000