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  • Title: Purification and characterization of beta-1,3-xylanase from a marine bacterium, Vibrio sp. XY-214.
    Author: Araki T, Tani S, Maeda K, Hashikawa S, Nakagawa H, Morishita T.
    Journal: Biosci Biotechnol Biochem; 1999 Nov; 63(11):2017-9. PubMed ID: 10635569.
    Abstract:
    beta-1,3-Xylanase was purified to gel electrophoretic homogeneity and 83-fold from a cell-free culture fluid of Vibrio sp. XY-214 by ammonium sulfate precipitation and successive chromatographies. The enzyme had a pl of 3.6 and a molecular mass of 52 kDa. The enzyme had the highest level of activity at pH 7.0 and 37 degrees C. The enzyme activity was completely inhibited by Cu2+, Hg2+, and N-bromosuccinimide. The enzyme hydrolyzed beta-1,3-xylan to produce mainly xylotriose and xylobiose but did not act on xylobiose, p-nitrophenyl-beta-D-xyloside, beta-1,4-xylan, beta-1,3-glucan, or carboxymethyl cellulose.
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