Title: Characterization of mannanase S1 from Klebsiella oxytoca KUB-CW2-3 and its application in copra mannan hydrolysis
Online: http:/­/­dspace.­library.­tu.­ac.­th…
Creator: Sudathip Titapoka Chantorn
Nawapan Pongsapipatana
Suttipan Keawsompong
Arunee Ingkakul
Haltrich, Dietmar
Sunee Nitisinprasert
Type: Article
Languge: en
Date: 2556-10-08T08:05:16Z
2013
Description: The mannanase S1 from Klebsiella oxytoca KUB-CW2-3 was purified by a single anion exchange chromatography to electrophoretic homogeneity. S1 is a protein with a molecular mass of approximately 165 kDa and a pI value of 3.5. The optimum pH and temperature of mannanase activity were 4.0 and 40 °C, respectively. The enzyme exhibited good stability over the broad pH range of 3-6. The mannanase S1 exhibited specific activity for different mannan substrates including galactomannan from locust bean gum (LBG), copra meal, and glucomannan from konjac, while neither xylanase nor cellulase activity were detectable. The Michaelis-Menten constants (Km), maximum velocity (Vmax), and the catalytic constant (kcat) values of S1 against LBG and konjac mannan were 1.038-1.056 mg/ml, 6.149-6.183 μU ml -1 min-1, and 0.047 s-1, respectively. In addition, mannanase activity was activated by Co2+ (129%) but completely inhibited by EDTA and Zn2+. The N-terminal amino acid sequence (GRVGEAGPHGPHGPH) of mannanase S1 is different from the N-terminal region of other bacterial mannanases belonging to the glycoside hydrolase family GH5. The degradation products of mannanase S1 from LBG hydrolysis were galactose and unknown oligosaccharides with a different molecular structure to mannobiose, triose, and tetraose indicating the cleavages of o-1,6-galactosidic and β-1,4-mannosidic linkages. Its hydrolysis of 100 mM CoCl2-treated copra mannan enhanced the growth of Lactobacillus reuteri KUB-AC5 but inhibited that of Salmonella serovar Enteritidis S003, indicating potential prebiotic properties by the action of mannanase from K. oxytoca.
Subject: β-mannanase
Copra meal
Prebiotics
Identifier: http://dspace.library.tu.ac.th/handle/3517/6712
Source: Thammasat Digital Library

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