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Enzymes of Aspergillus ochraceus and Their Applications
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This entry is adapted from the peer-reviewed paper 10.3390/molecules27196759

Fungus continues to attract great attention as a promising pool of biometabolites. Aspergillus ochraceus Wilh (Aspergillaceae) has established its capacity to biosynthesize a myriad of metabolites belonging to different chemical classes, such as isocoumarins, pyrazines, sterols, indole alkaloids, diketopiperazines, polyketides, peptides, quinones, polyketides, and sesquiterpenoids, revealing various bioactivities.

Aspergillus ochraceus Aspergillaceae fungi enzymes Biotechnological relevance

1. Introduction

Fungi are fascinating producers of various enzymes that have beneficial contributions in the industrial field. A. ochraceus produces a variety of enzymes, which are reviewed in this text, along with their possible biotechnological and industrial values.

2. Hydrolases

2.1. Glycoside Hydrolases

Lignocellulosic biomass is one of the alternative energy sources to fossil fuel that is composed of hemicelluloses, cellulose, and lignin [1][2][3][4]. Cellulases are the principal catalytic enzymes for lignocellulosic biomass hydrolysis, involving β-D-glucosidase, cellobiohydrolase, and endoglucanase, that synergistically hydrolyze cellulose into glucose [1][2][3][4]. They are applicable in the fermentation industry, which needs stability under extreme bioprocessing conditions and high yield. Coir pith or coconut pith is a byproduct of the coir industry with 25% cellulose that is possibly utilized as substrate for saccharification.
Asha et al. purified and characterized β-glucosidase (AS-HT-CeluzB) and processive-type endoglucanase (AS-HT-CeluzA) from A. ochraceus MTCC1810, which bio-converted delignified coir pith to glucose for subsequent bioethanol production [5]. These enzymes possessed optimal total cellulase (28.15 FPU/mL), endoglucanase (35.63 U/mL), and β-glucosidase (15.19 U/mL) capacities at pH 6/40 °C. Accordingly, these enzymes could be utilized as synergistic cellulases for complete cellulose saccharification in bio-refineries [5].
Xylan is a major component of the plant cell wall. It consists of 1,4-connected β-D-xylopyranose residues [1][2][3][4]. Xylanases facilitate xylan hydrolysis, primarily utilized in the kraft operation for removing the generated LCC (lignin–carbohydrate complex), which is a physical barrier towards bleaching chemicals entry [6]. Chemical bleaching relies on the utilization of a large quantity of chlorine and chlorine-related chemicals that results in bio-accumulating, mutagenic, toxic, and bio-harmful byproducts [7]. Alternatively, xylanases used in the paper and pulp industry is an eco-friendly method that minimizes pulp fibers’ damage and generates superior quality dissolving pulps [8]. The production of microbial xylanases using various lignocellulosic residues as growth substrates have received great attention because of its low cost and high yield [6][7][8].
Betini et al. reported the production of xylanases from A. ochraceus under SSF (solid-state fermentation) using agro-industrial residues (e.g., wheat bran, rice straw, oatmeal, corncob, and Eucalyptus grandis sawdust) [9]. It was found that xylanase production (20%) was favored when a mixture of corncob and wheat bran was utilized. The bio-bleaching assay of these enzymes revealed twice to thrice times increased brightness and maintained viscosity, indicating that their use could assist the reduction of chlorine compound concentration in cellulose pulp treatment [9]. In another study, A. ochraceus produced high levels of cellulase-free xylanase in oat spelt or birchwood xylan media using wheat bran residue. The enzyme had maximal activity at 65 °C and 5.0 pH [10]. It caused the bleaching of eucalyptus kraft pulp. The results could improve the economic characteristics of bio-bleaching technology and minimize the pollutant compounds used in the process [10]. In 2012, Michelin et al. studied the production of xylanase by A. ochraceus utilizing wheat straw autohydrolysis liquor as a carbon source [11]. It was found that the best yield of β-xylosidase and xylanase was obtained when A. ochraceus was cultivated with 1% wheat bran added to 10% wheat straw liquor in a stirred tank bioreactor, suggesting the possibility of scaling up this process for commercial production [11]. The enhancement of xylanase and p-xylosidase productivity by A. ochraceus using various chemical and physical mutagenesis was assessed [12]. It was found that the NG-13 (N-methyl-N′-nitro-N-nitrosoguanidine) mutant strain secreted high levels of β-xylosidase and xylanase during growth on agricultural waste and commercial xylan, which were stable with optimal activity at pH 5–10 and temperature 45–50 °C [12].
Invertases (β-D-fructo-furanosidases) hydrolyze polysaccharides and sucrose to produce glucose and fructose [13]. The resulting glucose and fructose mixture is called inverted sugar. Invertases are substantial in the food industry, particularly in confectionery for artificial sweetener preparation and increasing sweetening properties [13].
Ghosh et al. (2001) purified invertase enzymes from A. ochraceus that was thermotolerant with high sucrose and raffinose affinity [14]. A. ochraceus also produced high levels of an extracellular thermostable β-D-fructofuranosidase using sugar cane bagasse-supplemented Khanna medium at 40 °C [15]. This enzyme had a hydrolytic activity with no trans-fructosylating potential. Furthermore, it was positively affected by glucose, which distinguished it from the other β-d-fructofuranosidases, supporting its application for fructose syrup production and sucrose hydrolysis [15].

2.2. Proteolytic Enzymes

Medical interest has been drawn to the thrombolytic enzymes of microbial origin. These enzymes act directly by dissolving blood clots as plasmin or as blood plasminogen tissue activators [16]. Protein C prevents blood hyper-clotting in hemostasis [17]. Protein C activator’s addition to the blood inactivates clotting factors VIII and V, which are necessary for thrombin formation, resulting in the prolongation of the partial thromboplastin time [18]. Discovering protein C activators from microbes could be beneficial for clinical practice use because of the low cost.
From A. ochraceus 513, proteinase belonging to protein C activator types was separated and assessed for anti-coagulant and fibrinolytic potential [19]. This enzyme was efficient as Agkistrodon snake venom protein C activator in thrombin formation time prolongation [19]. Osmolovskiy et al. stated that extracellular proteinases produced by submerged cultures of a micromycete A. ochraceus L-1 exhibited specific fibrinogenolytic and fibrinolytic potential, whereas the highest effectiveness was observed at pH 7.0 and 28 °C [20].

2.3. Tannases

Tannases (tannin acyl hydrolase) catalyze the hydrolysis of depside and the ester bonds of hydrolyzable tannins [21]. They have been utilized as clarifying agents in the industrial processing of coffee-flavored soft drinks and fruit juices, instant teas manufacture, gallic acid production, and treatment of polyphenolics-contaminated wastewaters, as well as the removal of tannin from foodstuffs and animal feeds [22][23].
A. ochraceus was reported to yield extracellular thermostable tannase with distinctive monomeric structural characteristics. This enzyme was activated by manganese, revealing its biotechnological potential for gallic acid production [24]. Furthermore, it was found that A. ochraceus biofilm produced tannase in Khanna medium containing tannic acid (1.5% w/v, carbon source), which was higher than that obtained using conventional submerged fermentation. This enzyme exhibited potent effectiveness at pH 6.0 and 30 °C and was not affected by detergent and surfactant addition [25]. It had different biotechnological applications in propyl gallate production, tannin-rich leather effluent treatment, and sorghum feed formulation [25]. Thus, fungal biofilm is an interesting alternative to produce high levels of tannase with the biotechnological potential to be applied in different industrial sectors.

3. Oxidases

Alcohol oxidases catalyze the oxidation of alcohols to the corresponding carbonyl compounds with a concomitant release of hydrogen peroxide [26]. They have potential applications in biosensors and the biocatalytic production of different carbonyl compounds that are beneficial in pharmaceutical, flavor, and clinical industries [26]. A. ochraceus AIU031 secreted alcohol oxidase (AOD), belonging to the same group as methylotrophic yeast AOD. It oxidized short-chain primary alcohols and ethylene glycol [27]. It was found to possess an optimal ethanol oxidation capacity at 50–55 °C and pH 5–7 [27].

References

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  10. Michelin, M.; Peixoto-Nogueira, S.C.; Betini, J.; Da Silva, T.M.; Jorge, J.A.; Terenzi, H.F.; Polizeli, M. Production and Properties of Xylanases from Aspergillus terricola Marchal and Aspergillus ochraceus and their use in Cellulose Pulp Bleaching. Bioprocess Biosyst. Eng. 2010, 33, 813–821.
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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 : Rawan H. Hareeri ,
Mohammed M. Aldurdunji
, Hossam M. Abdallah , Ali A. Alqarni ,
Shaimaa G. A. Mohamed
, Gamal A. Mohamed , Sabrin R. M. Ibrahim
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Update Date: 16 Dec 2022
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