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Alkali-stable GH11 endo-b-1,4 xylanase (XynB) from Bacillus subtilis strain CAM 21: application in hydrolysis of agro-industrial wastes, fruit/vegetable peels and weeds.

Monica, P. and Mukesh, Kapoor (2020) Alkali-stable GH11 endo-b-1,4 xylanase (XynB) from Bacillus subtilis strain CAM 21: application in hydrolysis of agro-industrial wastes, fruit/vegetable peels and weeds. Preparative Biochemistry & Biotechnology.

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Abstract

GH11 endo-xylanases, due to their inherent structural and biochemical properties, are the key to efficient bioconversion of lignocellulosic biomass into value-added products. A GH11 endo-xylanase (XynB) from Bacillus subtilis strain CAM 21 was cloned, over-expressed and purified (Mw�24 kDa) using Ni-NTA affinity chromatography. XynB showed optimum activity at pH 7.0 and 50C and was stable (>88%) in a broad range of pH (4–11). The apparent Km, Kcat and Kcat/Km of XynB were 2.9 mg/ml, 1961.2/sec, and 675.62 ml/mg/sec, respectively using birchwood xylan as substrate. XynB was a classical endo-xylanase as it hydrolyzed birchwood xylan to xylo-oligosaccharides and not xylose. Kinetic stability of XynB at 45–53C was between 43-182 min. Secondary structure analysis of XynB using far-UV CD spectroscopy revealed presence of 51.85% b strands and 2.64% a helix and was consistent with the homology modeling studies. XynB hydrolyzed the xylan extracted from agro-industrial wastes and fruit/vegetable peels by releasing up to 670 mg/g of reducing sugars. The xylan extracted from weeds (Ageratum conyzoides, Achyranthes aspera and Tridax procumbens) had characteristic signatures of hemicelluloses and after XynB hydrolysis showed cracks, peeling and release of up to 135.2 mg/g reducing sugars.

Item Type: Article
Uncontrolled Keywords: Agro-industrial wastes; characterization; fruit/ vegetable peels; GH11 endo-b-14 xylanase; heterologous expression; hydrolysis; weeds
Subjects: 600 Technology > 08 Food technology > 16 Nutritive value > 05 Enzymes
600 Technology > 08 Food technology > 16 Nutritive value > 07 Waste utilization
Divisions: Protein Chemistry and Technology
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 04 Dec 2020 09:35
Last Modified: 04 Dec 2020 09:35
URI: http://ir.cftri.com/id/eprint/14706

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