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Purification and characterization of a novel a-D-glucosidase from Lactobacillus fermentum with unique substrate specificity towards resistant starch.

Mousami Shankar, A. and Muralikrishna, G. (2017) Purification and characterization of a novel a-D-glucosidase from Lactobacillus fermentum with unique substrate specificity towards resistant starch. The Journal of General and Applied Microbiology. pp. 1-7.

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Abstract

Resistant starch is not digestible in the small intestine and is fermented by lactic acid bacteria in the large intestine into short chain fatty acids, such as acetate, propionate and butyrate, which result in several health benefits in analogy with dietary fibre components. The mode and mechanism of resistant starch degradation by lactic acid bacteria is still not understood. In the present study, we have purified a-D-glucosidase from Lactobacillus fermentum NCDC 156 by employing three sequential steps i.e. ultra filtration, DEAE-cellulose and Sephadex G-100 chromatographies. It was found to be a monomeric protein (~50 kDa). The optimum pH and temperature of this enzyme were found to be 5.5 and 37∞C, respectively. Under optimised conditions with p-nitrophenyl-D-glucopyranoside as the substrate, the enzyme exhibited a Km of 0.97 mM. Its activity was inhibited by Hg2+ and oxalic acid. N-terminal blocked purified enzyme was subjected to lysyl endopeptidase digestion and the resultant peptides were subjected to BLAST analysis to understand their homology with other a-Dglucosidases from lactobacillus species.

Item Type: Article
Uncontrolled Keywords: a-D-glucosidase; Lactobacillus fermentum; N-terminal amino acid analysis; purification; resistant starch
Subjects: 500 Natural Sciences and Mathematics > 04 Chemistry and Allied Sciences > 28 Polysaccharide Chemistry
500 Natural Sciences and Mathematics > 07 Life Sciences > 04 Microbiology > 02 Bacteriology
Divisions: Dept. of Biochemistry
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 19 Jan 2018 05:39
Last Modified: 19 Jan 2018 05:39
URI: http://ir.cftri.com/id/eprint/13331

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