Cloning and characterization of a novel cellobiase gene, cba3, encoding the first known β-glucosidase of glycoside hydrolase family 1 of Cellulomonas biazotea

Chan, Anthony; Wang, Yule Yue; Ng, Ka Lun; Fu, Zhibiao; Wong, Wan Keung

doi:10.1016/j.gene.2011.11.027

Cited by 8 publications

(14 citation statements)

References 41 publications

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“…To obtain an improved enzyme, researchers have adopted several approaches like heterogeneous expression of β-glucosidase genes from different sources (Byeon et al 2005 ; Chan et al 2011 ; Aftab et al 2012 ), characterization of immobilized enzyme in several agents (Keerti et al 2014 ) and side-directed mutagenesis to enhance the efficacy of enzymes (Wang et al 1995 ; Liu et al 2011 ; Agrawal et al 2012 ). Cloning and expression in suitable host for bulk production of β-glucosidase enzyme is one of the primitive concerns about ongoing research on β-glucosidase.…”

Section: Isolation Cloning and Expression Studies For Production Of mentioning

confidence: 99%

“…of Amino acids pH optima Temp. optima (°C) GH family References Bacteria Acetobacter xylinum E. coli 79 739 – – GH3 Tajima et al ( 2001 ) Vibrio cholera E. coli 65 574 6.0–6.5 37–42 GH9 Park et al ( 2002 ) Thermus flavus E. coli 49 431 5.0–6.0 80–90 GH1 Kang et al ( 2005 ) Thermus thermophiles E. coli 48.7 431 8.5 90 GH1 Gu et al ( 2009 ) Exiguobacterium oxidotolerans E. coli 51.6 448 7 35 GH1 Chen et al ( 2010a ) Cellulomonas biazotea E. coli 48 447 – – GH1 Chan et al ( 2011 ) Exiguobacterium ...…”

Section: Isolation Cloning and Expression Studies For Production Of mentioning

confidence: 99%

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Catalytic properties, functional attributes and industrial applications of β-glucosidases

2015

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β-Glucosidases are diverse group of enzymes with great functional importance to biological systems. These are grouped in multiple glycoside hydrolase families based on their catalytic and sequence characteristics. Most studies carried out on β-glucosidases are focused on their industrial applications rather than their endogenous function in the target organisms. β-Glucosidases performed many functions in bacteria as they are components of large complexes called cellulosomes and are responsible for the hydrolysis of short chain oligosaccharides and cellobiose. In plants, β-glucosidases are involved in processes like formation of required intermediates for cell wall lignification, degradation of endosperm’s cell wall during germination and in plant defense against biotic stresses. Mammalian β-glucosidases are thought to play roles in metabolism of glycolipids and dietary glucosides, and signaling functions. These enzymes have diverse biotechnological applications in food, surfactant, biofuel, and agricultural industries. The search for novel and improved β-glucosidase is still continued to fulfills demand of an industrially suitable enzyme. In this review, a comprehensive overview on detailed functional roles of β-glucosidases in different organisms, their industrial applications, and recent cloning and expression studies with biochemical characterization of such enzymes is presented for the better understanding and efficient use of diverse β-glucosidases.

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Section: Isolation Cloning and Expression Studies For Production Of mentioning

confidence: 99%

Section: Isolation Cloning and Expression Studies For Production Of mentioning

confidence: 99%

Catalytic properties, functional attributes and industrial applications of β-glucosidases

2015

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“…Enzymes from GH1 are good candidates for true cellobiase activity from a variety of organisms (33)(34)(35), so we reasoned that the Celf_2783 protein was a candidate cellobiase. A GH1 cellobiase from C. biazotea has recently been examined, but the complete substrate specificity profile and enzymatic characterization have not been published (36). There is also a GenBank entry for a GH1 from C. fimi (AAA23091.1), which differs in amino acid sequence from the protein encoded by Celf_2783 (the genome-derived GH1), and we were unable to find published biochemical data about this protein.…”

Section: Discussionmentioning

confidence: 98%

Characterization of Five β-Glycoside Hydrolases from Cellulomonas fimi ATCC 484

Gao

Wakarchuk

2014

J Bacteriol

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bThe Gram-positive bacterium Cellulomonas fimi produces a large array of carbohydrate-active enzymes. Analysis of the collection of carbohydrate-active enzymes from the recent genome sequence of C. fimi ATCC 484 shows a large number of uncharacterized genes for glycoside hydrolase (GH) enzymes potentially involved in biomass utilization. To investigate the enzymatic activity of potential ␤-glucosidases in C. fimi, genes encoding several GH3 enzymes and one GH1 enzyme were cloned and recombinant proteins were expressed in Escherichia coli. Biochemical analysis of these proteins revealed that the enzymes exhibited different substrate specificities for para-nitrophenol-linked substrates (pNP), disaccharides, and oligosaccharides. Celf_2726 encoded a bifunctional enzyme with ␤-D-xylopyranosidase and ␣-L-arabinofuranosidase activities, based on pNPlinked substrates (CfXyl3A). Celf_0140 encoded a ␤-D-glucosidase with activity on ␤-1,3-and ␤-1,6-linked glucosyl disaccharides as well as pNP-␤-Glc (CfBgl3A). Celf_0468 encoded a ␤-D-glucosidase with hydrolysis of pNP-␤-Glc and hydrolysis/transglycosylation activities only on ␤-1,6-linked glucosyl disaccharide (CfBgl3B). Celf_3372 encoded a GH3 family member with broad aryl-␤-D-glycosidase substrate specificity. Celf_2783 encoded the GH1 family member (CfBgl1), which was found to hydrolyze pNP-␤-Glc/Fuc/Gal, as well as cellotetraose and cellopentaose. CfBgl1 also had good activity on ␤-1,2-and ␤-1,3-linked disaccharides but had only very weak activity on ␤-1,4/6-linked glucose.

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“…Để thu nhận và nâng cao hoạt tính enzyme, một số phương pháp như biểu hiện các gen mã hóa βglucosidase từ các nguồn khác nhau đã được công bố (Byeon et al, 2005;Chan et al, 2012;Tang et al, 2014). Việc tìm kiếm chủng chủ phù hợp để sản xuất lượng lớn enzyme là một trong những mối quan tâm hàng đầu.…”

Section: Mở đầUunclassified

Improvement of a recombinant β-glucosidase activity of a sequence derived from metagenome database of Binh Chau hotspring

Thủy

Nhung

Xuan

et al. 2020

Vietnam J. Biotechnol.

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Metabolic products obtaining from microorganisms of geothermal ecologies often show special characteristics which help their cells to survive, grow and develop under extreme conditions. Exploiting the microbial gene resource of those environments demands a new approach via uncultured methods. Thanks to the development of metagenomics and bioinformatic softwares, we can exploit novel genes from environment directly. Based on Binh Chau hotspring’s DNA metagenome sequencing, ORF [denovogenes]_32768 encoding for β-glucosidase is selected for expression into pET17b vector because it shown a low similartity of amino acid sequence as compared to others in Genbank, a high alkali and Tm predicted values. To improve the expression efficiency of β-glucosidase, some factors (host strains, medium culture, IPTG concentration, aeration…) are investigated. The results showed that the recombinant E. coli C43(DE3) reached the highest dried biomass at 8.26 g/L and the maximum enzymatic activity at 0.34 U/mL in shaking condition (TB medium plus 0.25 mM IPTG with the ratio of cultured /flask volume is 20%, 42-48 hours, 30°C). This study demonstrates the capacity of mining a novel gene encoded for enzyme from DNA metagenome of Vietnam hot spring as well as produces recombinant enzyme for biomass conversion.

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Cloning and characterization of a novel cellobiase gene, cba3, encoding the first known β-glucosidase of glycoside hydrolase family 1 of Cellulomonas biazotea

Cited by 8 publications

References 41 publications

Catalytic properties, functional attributes and industrial applications of β-glucosidases

Catalytic properties, functional attributes and industrial applications of β-glucosidases

Characterization of Five β-Glycoside Hydrolases from Cellulomonas fimi ATCC 484

Improvement of a recombinant β-glucosidase activity of a sequence derived from metagenome database of Binh Chau hotspring

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