Literature DB >> 27558695

Bifunctional recombinant cellulase-xylanase (rBhcell-xyl) from the polyextremophilic bacterium Bacillus halodurans TSLV1 and its utility in valorization of renewable agro-residues.

Gurdeep Rattu1, Swati Joshi1, T Satyanarayana2.   

Abstract

The thermostable bifunctional CMCase and xylanase encoding gene (rBhcell-xyl) from Bacillus halodurans TSLV1 has been expressed in Escherichia coli. The recombinant E. coli produced rBhcell-xyl (CMCase 2272 and 910 U L-1 xylanase). The rBhcell-xyl is a ~62-kDa monomeric protein with temperature and pH optima of 60 °C and 6.0 with T1/2 of 7.0 and 3.5 h at 80 °C for CMCase and xylanase, respectively. The apparent K m values (CMC and Birchwood xylan) are 3.8 and 3.2 mg mL-1. The catalytic efficiency (k cat/K m ) values of xylanase and CMCase are 657 and 171 mL mg-1 min-1, respectively. End-product analysis confirmed that rBhcell-xyl is a unique endo-acting enzyme with exoglucanase activity. The rBhcell-xyl is a GH5 family enzyme possessing single catalytic module and carbohydrate binding module. The action of rBhcell-xyl on corn cobs and wheat bran liberated reducing sugars, which can be fermented to bioethanol and fine biochemicals.

Entities:  

Keywords:  Agro-residues; Bacillus halodurans TSLV1; Enzymatic saccharification; Recombinant bifunctional cellulase–xylanase; Xylo-oligosaccharides and cello-oligosaccharides

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Year:  2016        PMID: 27558695     DOI: 10.1007/s00792-016-0870-6

Source DB:  PubMed          Journal:  Extremophiles        ISSN: 1431-0651            Impact factor:   2.395


  34 in total

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2.  A novel thermostable GH10 xylanase with activities on a wide variety of cellulosic substrates from a xylanolytic Bacillus strain exhibiting significant synergy with commercial Celluclast 1.5 L in pretreated corn stover hydrolysis.

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Review 5.  Multifunctional cellulases are potent, versatile tools for a renewable bioeconomy.

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  5 in total

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