Cellulose is the most abundant biopolymer in biosphere and the major constituent of plant biomass. Cellulose polymer is made up of β-glucose units linked by β-glucosidic bonds. Cellulase is an enzymatic system that catalyzes the hydrolysis of cellulose polymer to glucose monomers. This enzymatic system consists of three individual enzymes namely endoglucanase, exoglucanase and β-glucosidase which act synergistically to degrade cellulose molecules into glucose. Cellulases are produced by bacteria, fungi, plants, and animals and used in many industrial applications such as textile industries, laundry and detergent industries, paper and pulp industry, animal feeds, and biofuels production. β-Glucosidase is a diverse group of enzymes with wide distribution in bacteria, fungi, plants and animals and has the potential to be utilized in various biotechnological processes such as biofuel production, isoflavone hydrolysis, flavor enhancement and alkyl/aryl β-D-glucoside and oligosaccharides synthesis. Thus, there is increased demand of β-glucosidase production from microbial sources under profitable industrial conditions. In this review, β-glucosidase classification, localization, and mechanism of action will be described. Subsequently, the various sources of β-glucosidase for industrial sector will be discussed. Moreover, Fermentation methods and various parameters affecting β-glucosidase production will be highlighted on the light of recent findings of different researchers. Finally, β-glucosidase applications in biofuel production, flavors enhancement, isoflavones hydrolysis, cassava detoxification and oligosaccharide synthesis will be described.

Microbial β-Glucosidase: sources, production and applications / Ahmed, Amer; Nasim Faiz, ul-Hassan; Batool, Kashfa; Bibi, Aasia. - In: JOURNAL OF APPLIED & ENVIRONMENTAL MICROBIOLOGY. - ISSN 2373-6747. - 5:1(2017), pp. 31-46.

Microbial β-Glucosidase: sources, production and applications

Bibi Aasia
2017

Abstract

Cellulose is the most abundant biopolymer in biosphere and the major constituent of plant biomass. Cellulose polymer is made up of β-glucose units linked by β-glucosidic bonds. Cellulase is an enzymatic system that catalyzes the hydrolysis of cellulose polymer to glucose monomers. This enzymatic system consists of three individual enzymes namely endoglucanase, exoglucanase and β-glucosidase which act synergistically to degrade cellulose molecules into glucose. Cellulases are produced by bacteria, fungi, plants, and animals and used in many industrial applications such as textile industries, laundry and detergent industries, paper and pulp industry, animal feeds, and biofuels production. β-Glucosidase is a diverse group of enzymes with wide distribution in bacteria, fungi, plants and animals and has the potential to be utilized in various biotechnological processes such as biofuel production, isoflavone hydrolysis, flavor enhancement and alkyl/aryl β-D-glucoside and oligosaccharides synthesis. Thus, there is increased demand of β-glucosidase production from microbial sources under profitable industrial conditions. In this review, β-glucosidase classification, localization, and mechanism of action will be described. Subsequently, the various sources of β-glucosidase for industrial sector will be discussed. Moreover, Fermentation methods and various parameters affecting β-glucosidase production will be highlighted on the light of recent findings of different researchers. Finally, β-glucosidase applications in biofuel production, flavors enhancement, isoflavones hydrolysis, cassava detoxification and oligosaccharide synthesis will be described.
2017
cellulose; glycoside hydrolase; cellulase; β-glucosidase; biofuel; transglycosylation
01 Pubblicazione su rivista::01g Articolo di rassegna (Review)
Microbial β-Glucosidase: sources, production and applications / Ahmed, Amer; Nasim Faiz, ul-Hassan; Batool, Kashfa; Bibi, Aasia. - In: JOURNAL OF APPLIED & ENVIRONMENTAL MICROBIOLOGY. - ISSN 2373-6747. - 5:1(2017), pp. 31-46.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/1227144
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