Endoxanthanase, a Novel β-d-Glucanase Hydrolyzing Backbone Linkage of Intact Xanthan from Newly Isolated Microbacterium sp. XT11

Endoxanthanase, a Novel β-d-Glucanase Hydrolyzing Backbone Linkage of Intact Xanthan from Newly Isolated Microbacterium sp. XT11

A novel endoxanthanase was produced and isolated from the culture of Microbacterium sp. XT11 growing on xanthan. Optimum pH and temperature for the enzyme activity were 6.0 and 35-40 °C, respectively. The endoxanthanase cleaves the backbone endo-β-1,4-glucosidic linkage of the xanthan molecule, whic...

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Veröffentlicht in:Applied biochemistry and biotechnology 2009-10, Vol.159 (1), p.24-32
Hauptverfasser: Li, Bing, Guo, Jiqiang, Chen, Wenfu, Chen, Xiaoyi, Chen, Ligang, Liu, Zhiwen, Li, Xianzhen
Format: Artikel
Sprache:eng
Schlagworte:
beta-glucanase
Binding Sites
Biochemistry
Biological and medical sciences
Biotechnology
Chemistry
Chemistry and Materials Science
Endo-1,3-beta-Glucanase - chemistry
enzymatic hydrolysis
Enzyme Activation
Enzyme Stability
food industry
Fundamental and applied biological sciences. Psychology
glycosidic linkages
Gram-Positive Bacteria - enzymology
Hydrolysis
Microbacterium
Polysaccharides, Bacterial - chemistry
Protein Binding
xanthan gum
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Zusammenfassung:A novel endoxanthanase was produced and isolated from the culture of Microbacterium sp. XT11 growing on xanthan. Optimum pH and temperature for the enzyme activity were 6.0 and 35-40 °C, respectively. The endoxanthanase cleaves the backbone endo-β-1,4-glucosidic linkage of the xanthan molecule, which is specific to the intact xanthan. However, the lyase-treated xanthan or carboxymethyl cellulose could not be cleaved by endoxanthanase.
ISSN:0273-2289
1559-0291
DOI:10.1007/s12010-008-8439-1