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Characterization of purified xylanase from finger millet (Eleusine coracana-Indaf 15) malt

Chithra, M. and Muralikrishna, G. (2008) Characterization of purified xylanase from finger millet (Eleusine coracana-Indaf 15) malt. European Food Research and Technology, 227. pp. 587-597.

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Xylanase (E.C. was purified to apparent homogeneity from 96 h finger millet (Eleusine coracana, Indaf-15) malt by a three step purification procedure via ammonium sulphate fractionation, DEAEcellulose ion exchange and Sephadex G-75 gel permeation chromatographies with a recovery of 4.0% and fold puri- fication of 60. Xylanase, having a molecular weight of 29 ± 2 kDa was found to be monomeric on SDS-PAGE. pH optimum of the enzyme was found to be in the range of 5.0–5.5. The activation energy was 25 kJmol–1. Xylanase showed maximum stability at 35 �C in a pH range of 5.0– 6.0. Km and Vmax of purified xylanase were found to be 0.2% and 4.5 lmol min–1, respectively. Metal ions such as Ca2+, Mg2+, Mn2+, Cu2+, Fe2+, Ag2+ and Ni2+ enhanced xylanase activity at 5 mM concentration. p-chloromercuribenzoate, citric, oxalic and boric acids inhibited the enzyme in concentration dependent manner. The mode of action of xylanase was found to be ‘‘endo’’ as determined by the analysis of products liberated from larchwood xylan by ESI-MS and H1NMR. In vitro studies using Bifidobacterium and Lactobacillus sp. confirmed the prebiotic activity of the xylo-oligosaccharides.

Item Type: Article
Uncontrolled Keywords: Xylanase � Finger millet � Purification � Xylo-oligosaccharides � Prebiotic activity
Subjects: 600 Technology > 08 Food technology > 16 Nutritive value > 05 Enzymes
600 Technology > 08 Food technology > 21 Cereals > 05 Ragi (Finger Millet)
Divisions: Dept. of Biochemistry
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 09 Aug 2008 10:35
Last Modified: 15 Dec 2017 06:13
URI: http://ir.cftri.com/id/eprint/8679

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