Secretion of recombinant thermo-alkali-stable endoxylanase of polyextremophilic Bacillus halodurans TSEV1 and its utility in generating xylooligosaccharides from renewable agro-residues

Kumar, Vikash; Satyanarayana, T.

doi:10.1016/j.procbio.2014.08.012

Cited by 5 publications

(1 citation statement)

References 41 publications

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“…This domain can promote the affinity of enzymes toward their substrates. In addition, it may promote synergies with a multi-enzyme system to degrade the substrate (Shin et al 2002;Kumar and Satyanarayana 2014).…”

Section: Introductionmentioning

confidence: 99%

Inter domain interactions influence the substrate affinity and hydrolysis product specificity of xylanase from Streptomyces chartreusis L1105

et al. 2020

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Purpose: This study investigated the influence of inter-domain interactions on the substrate affinity and hydrolysis product specificity of xylanase. Methods: Genes encoding a GH10 endo-xylanase from Streptomyces chartreusis L1105 xynA and its truncated derivative were cloned and expressed in Escherichia coli. The catalytic activities of the enzyme (xynA) and the derivative xynADCBM, lacking the carbohydrate binding module (CBM), were assessed to evaluate the role of CBM in xynA. Results: Recombinant xynA (44 kDa) was found to be optimally active on beechwood xylan at 65°C with pH 7.7, while xynADCBM (34 kDa) exhibited optimal activity at 65°C with pH 7.2. Additionally, xynA and xynADCBM were found to be highly thermostable at 40-60°C, each retaining 80% of their original activity after 30 min. The xynADCBM without the CBM domain was highly efficient at hydrolyzing xylan to produce xylobiose (over 67%), which may be because the CBM domain facilitates substrate binding with xylanase. Meanwhile, the xylan hydrolysis efficiency of xynADCBM was higher than that of xynA. Conclusion: These findings showed that the CBM domain with non-catalytic activity has no significant effect on the characteristics of the enzyme at optimum pH and pH tolerance. It has also been suggested that the derivative xynADCBM without CBM components can promote hydrolysis of xylan to yield xylooligosaccharides, which has great potential economic benefits.

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Section: Introductionmentioning

confidence: 99%

Inter domain interactions influence the substrate affinity and hydrolysis product specificity of xylanase from Streptomyces chartreusis L1105

et al. 2020

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Technical Developments for Vegetable Waste Biomass Degradation by Thermophiles

Poli

Finore

Tramice

et al. 2016

Grand Challenges in Biology and Biotechnology

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Production of Ca2+-Independent and Acidstable Recombinant α-Amylase of Bacillus acidicola Extracellularly and its Applicability in Generating Maltooligosaccharides

Parashar

Satyanarayana

2016

Mol Biotechnol

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The recombinant acidstable α-amylase (Ba-amy) of acidophilic bacterium Bacillus acidicola TSAS1 has been produced extracellularly using a combination of cloning (E. coli and P. pastoris) and physico-chemical treatment strategies. A total of 150,000 U/L of Ba-amy were attained under constitutive promoter in P. pastoris, which is 15-fold higher than that of the wild strain B. acidicola (10,000 U/L). The recombinant P. pastoris integrated two copies of Ba-amy under GAP promoter. The pure Ba-amy expressed in P. pastoris is a glycoprotein of 66 kDa, which is optimally active at pH 4.0 and 60 °C with a T of 25 min at 70 °C. The K, V and K values of the recombinant Ba-amy are 1.66 mg/mL, 53.6 µmol/mg/min and 106.8/s, respectively. The enzyme generates maltose (30 %), maltotriose (20 %) and other higher maltooligosaccharides from starch, thus, useful in baking as an antistale. This is the first report on the optimization of extracellular production of recombinant acidic α-amylase of an acidophilic bacterium.

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Secretion of recombinant thermo-alkali-stable endoxylanase of polyextremophilic Bacillus halodurans TSEV1 and its utility in generating xylooligosaccharides from renewable agro-residues

Cited by 5 publications

References 41 publications

Inter domain interactions influence the substrate affinity and hydrolysis product specificity of xylanase from Streptomyces chartreusis L1105

Inter domain interactions influence the substrate affinity and hydrolysis product specificity of xylanase from Streptomyces chartreusis L1105

Technical Developments for Vegetable Waste Biomass Degradation by Thermophiles

Production of Ca2+-Independent and Acidstable Recombinant α-Amylase of Bacillus acidicola Extracellularly and its Applicability in Generating Maltooligosaccharides

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