Characterization of Xyn30A and Axh43A of Bacillus licheniformis SVD1 identified by its genomic analysis

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• 作者：Makiko Sakka ; Satoshi Tachino ; Hirotaka Katsuzaki ; J. Susan van Dyk ; Brett I. Pletschke ; Tetsuya Kimura ; Kazuo Sakka
• 关键词：Arabinofuranosidase ; Bacillus licheniformis ; Genome ; Multienzyme complex ; Xylanase
• 刊名：Enzyme and Microbial Technology
• 出版年：2012
• 出版时间：10 September, 2012
• 年：2012
• 卷：51
• 期：4
• 页码：193-199
• 全文大小：558 K

文摘

The genome sequence of Bacillus licheniformis SVD1, that produces a cellulolytic and hemi-cellulolytic multienzyme complex, was partially determined, indicating that the glycoside hydrolase system of this strain is highly similar to that of B. licheniformis ATCC14580. All of the fifty-six genes encoding glycoside hydrolases identified in B. licheniformis ATCC14580 were conserved in strain SVD1. In addition, two new genes, xyn30A and axh43A, were identified in the B. licheniformis SVD1 genome. The xyn30A gene was highly similar to Bacillus subtilis subsp. subtilis 168 xynC encoding for a glucuronoarabinoxylan endo-1,4-¦Â-xylanase. Xyn30A, produced by a recombinant Escherichia coli, had high activity toward 4-O-methyl-d-glucurono-d-xylan but showed definite activity toward oat-spelt xylan and unsubstituted xylooligosaccharides. Recombinant Axh43A, consisting of a family-43 catalytic module of the glycoside hydrolases and a family-6 carbohydrate-binding module (CBM), was an arabinoxylan arabinofuranohydrolase (¦Á-l-arabinofuranosidase) classified as AXH-m23 and capable of releasing arabinosyl residues, which are linked to the C-2 or C-3 position of singly substituted xylose residues in arabinoxylan or arabinoxylan oligomers. The isolated CBM polypeptide had an affinity for soluble and insoluble xylans and removal of the CBM from Axh43A abolished the catalytic activity of the enzyme, indicating that the CBM plays an essential role in hydrolysis of arabinoxylan.