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Catalytic Properties, Functional Attributes and Industrial Applications of B-Glucosidases

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Catalytic Properties, Functional Attributes and Industrial Applications of B-Glucosidases 3 Biotech (2016) 6:3 DOI 10.1007/s13205-015-0328-z ORIGINAL ARTICLE Catalytic properties, functional attributes and industrial applications of b-glucosidases 1 2 3 Gopal Singh • A. K. Verma • Vinod Kumar Received: 20 April 2015 / Accepted: 19 June 2015 / Published online: 31 December 2015 Ó The Author(s) 2015. This article is published with open access at Springerlink.com Abstract b-Glucosidases are diverse group of enzymes with biochemical characterization of such enzymes is with great functional importance to biological systems. presented for the better understanding and efficient use of These are grouped in multiple glycoside hydrolase families diverse b-glucosidases. based on their catalytic and sequence characteristics. Most studies carried out on b-glucosidases are focused on their Keywords b-Glucosidases Á Glycoside hydrolase Á industrial applications rather than their endogenous func- Cellulosome Á Glucosides Á Cellulase tion in the target organisms. b-Glucosidases performed many functions in bacteria as they are components of large complexes called cellulosomes and are responsible for the Introduction hydrolysis of short chain oligosaccharides and cellobiose. In plants, b-glucosidases are involved in processes like b-Glucosidases (b-D-glucopyrranoside glucohydrolase) formation of required intermediates for cell wall lignifi- [E.C.3.2.1.21] are the enzymes which hydrolyze the gly- cation, degradation of endosperm’s cell wall during ger- cosidic bond of a carbohydrate moiety to release nonre- mination and in plant defense against biotic stresses. ducing terminal glycosyl residues, glycoside and Mammalian b-glucosidases are thought to play roles in oligosaccharides (Bhatia et al. 2002; Morant et al. 2008; metabolism of glycolipids and dietary glucosides, and Cairns and Esen 2010; Li et al. 2013). These enzymes are signaling functions. These enzymes have diverse biotech- present in all kinds of organisms including bacteria, nological applications in food, surfactant, biofuel, and archaea, and eukaryotes, and play several important roles agricultural industries. The search for novel and improved such as biomass conversion in microorganisms, breakdown b-glucosidase is still continued to fulfills demand of an of glycolipids and process of lignification, involve in industrially suitable enzyme. In this review, a compre- defense against pests, phytohormones activation, catabo- hensive overview on detailed functional roles of b-glu- lism of cell wall in plants and both plant–microbes and cosidases in different organisms, their industrial plant–insects interaction. b-Glucosidase also plays an applications, and recent cloning and expression studies important role in the treatment of Gaucher’s disease (re- sulting from a deficiency of b-glucosidase) in which accumulation of glycoceramides takes place in the lyso- & Vinod Kumar somal tissues (Butters 2007). b-Glucosidases are the [email protected] essential part of cellulase system (cellulose metabolizing enzymes) and catalyze the last and final step in cellulose 1 Institute of Himalayan Bioresource Technology, Palampur 176062, India hydrolysis. Cellulase enzymes hydrolyze the cellulose to produce cellobiose and other short oligosaccharides which 2 Department of Biochemistry, College of Basic Sciences and Humanities, G. B. Pant University of Agriculture and are finally hydrolyzed to glucose by b-glucosidase. All the Technology, Pantnagar 263145, India enzymes, which are involved in cellulose hydrolysis, are 3 Department of Biotechnology, Akal College of Agriculture, normally grouped as cellulase system (Fig. 1). It consists of Eternal University, Baru Sahib, Sirmour 173101, India the following enzymes: endoglucanase (endo-1, 4–b- 123 3 Page 2 of 14 3 Biotech (2016) 6:3 Fig. 1 Diagrammatic overview of cellulose metabolism by cellulase smaller sized oligosaccharides. These smaller molecules are finally system: during cellulose hydrolysis, cellulase along with exo and utilized by b-glucosidase as a substrate to release glucose as the final endoglucanase acts on the cellulosic fibers and hydrolyzed it into the product of complete hydrolysis of cellulosic substance glucanase [E.C.3.2.1.4]), exoglucanase (cellobiohydrolase) role in flavor liberation from glucosylated (b-glucosides (exo-1, 4-b-glucanase [E.C.3.2.1.91]) and b-glucosidase conjugated) precursors in fruits and other plant tissues (b-D-glucoside glycohydrolase [E.C.3.2.1.21]) (Teeri (Krisch et al. 2010). Cleavage of phenolic and phytoe- 1997). The endoglucanase randomly hydrolyzes the b–1–4 strogen glucosides from fruits and vegetables is also car- bonds in the middle portion of cellulose molecule and the ried out by applying this enzyme to extract medicinally exoglucanase acts at reducing and non-reducing ends to important compounds and to enhance the quality of bev- release the cellobiose and other oligosaccharides. Finally, erages (Schroder et al. 2014). b-Glucosidases hydrolyzed these oligosaccharides are converted to glucose by b-glu- anthocyanine products, i.e., anthocyanidins and sugar cosidase (Bhat and Bhat 1997). aglycones are less soluble than anthocyanines, possess little b-Glucosidases are widely used in the various biotech- colour, tend to precipitate and can be removed more easily. nological processes, including the production of biofuel b-Glucosidases can improve the organoleptic properties of and ethanol from cellulosic agricultural wastes and syn- citrus fruits and juices in which bitterness is in part due to a thesis of useful b-glucosides (Li et al. 2013). These glucosidic compound, naringin whose hydrolysis requires enzymes are employed in industry for hydrolysis of bitter in succession, an a-rhamnosidase and a b-glucosidase compounds during juice extraction and liberation of aroma (Riou et al. 1998). b-Glucosidases have been the subject of from wine grapes (Gueguen et al. 1998; Harhangi et al. recent research due to the key role of these enzymes in 2002). In flavor industry, b-glucosidases are the key biological processes and for many biotechnological appli- enzymes in the enzymatic release of aromatic compounds cations. In present review, we briefly explain the general- from glucosidic precursors present in fruits and fermenting ized action mechanisms of b-glucosidase enzymes, their products (Krisch et al. 2010). Also, this has large potential functional role in different types of organisms and signif- for application in food processing industries and used as a icant contribution in different industries along with a brief flavor enzyme to enhance the flavor of wine, tea and fruit look on the current research for improving the efficiency of juice (Keerti et al. 2014). b-Glucosidases play an important this industrially important enzyme. 123 3 Biotech (2016) 6:3 Page 3 of 14 3 Types of b-glucosidases and their classification barrel Folds as a key feature of GH1 family b-glucosidase was reported in X-ray crystallographic structure of b-glu- b-Glucosidases are common among plants, fungi and cosidase BGL1A from a basidiomycete (Phanerochaete bacteria, and showed an identical similarity with respect to chrysosporium) by Nijikken et al. (2007). Structure of their sequences and structures. They can be classified on human cytosolic b-glucosidase was also illustrated by the basis of their substrate activity or their nucleotide X-ray crystallography and reported the existence of the sequence identity. Based on substrate specificity, b-glu- same (b/a)8 barrel (Tribolo et al. 2007). cosidases are grouped into three classes: (i) aryl-b-D-glu- cosidases (having strong affinity for aryl-b-D-glucosides), (ii) cellobiases (hydrolyze only disaccharides) and (iii) Catalytic mechanism of b-glucosidases broad specificity glucosidases (exhibit activity on many substrate types and are the most commonly found b-glu- For elucidating the catalytic mechanism of the enzyme and cosidases) (Rajan et al. 2004). On the basis of sequence the active site topology, several techniques such as pH- homology, b-glucosidases have been divided into two sub- dependence, inhibition, isotopic effect, and structure–re- families (i) BGA (b-glucosidases and phospho-b-glucosi- activity studies (Kempton and Withers 1992), essential dases from bacteria to mammals) and (ii) BGB (b-glu- amino acid labeling with fluorosugars (Withers et al. 1992), cosidases from yeasts, molds and rumen bacteria) (Cantarel reactions with deoxy substrate analogues (Street et al. et al. 2009; Krisch et al. 2010). An alternative classification 1992), and site-directed mutagenesis (Wang et al. 1995) system for glycoside hydrolases based on amino acid have been used. b-Glucosidases cleave b-glycosidic bonds sequence and structural similarity has also been developed between two or more carbohydrates, or between a carbo- (Henrissat and Davies 1997). In this system, those enzymes hydrate and a non-carbohydrate moiety (http://www.cazy. with overall amino acid sequence similarity and well- org/Glycoside-Hydrolases.html). Most b-glucosidases that conserved sequence motifs are considered in a single have been characterized (i.e., GH1, GH3 and GH30 family family. At present, 133 glycoside hydrolase (GH) families enzymes) are retaining enzymes, and they perform catal- are listed in the frequently updated Carbohydrate Active ysis in two steps, glycosylation and deglycosylation. Their enZYme (CAZY) website (http://www.cazy.org) (Cantarel catalytic mechanism is described diagrammatically in et al. 2009; Cairns and Esen 2010). These families are Fig. 2. Glutamate is the key active site residue and con-
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