Abstract:
:An alginate lyase gene, algA, encoding a new poly β-D-mannuronate (polyM)-specific alginate lyase AlgA, was cloned from Pseudomonas sp. E03. The recombinant AlgA with (His)6-tag, consisting of 364 amino acids (40.4 kDa),was purified using Ni-NTA Sepharose. The purified lyase had maximal activity (222 EU/mg) at pH 8 and 30 °C and also maintained activity between pH 7-9 and below 45 °C. It exclusively and endolytically depolymerized polyM by β-elimination into oligosaccharides with degrees of polymerization (DP) of 2-5. Due to its high substrate specificity, AlgA could be a valuable tool for production of polyM oligosaccharides with low DP and for determining the fine structure of alginate.
journal_name
Biotechnol Lettjournal_title
Biotechnology lettersauthors
Zhu BW,Huang LS,Tan HD,Qin YQ,Du YG,Yin Hdoi
10.1007/s10529-014-1685-0subject
Has Abstractpub_date
2015-02-01 00:00:00pages
409-15issue
2eissn
0141-5492issn
1573-6776journal_volume
37pub_type
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pub_type: 杂志文章
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pub_type: 杂志文章
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更新日期:2007-02-01 00:00:00
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更新日期:2003-03-01 00:00:00
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更新日期:2006-07-01 00:00:00
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更新日期:2018-04-01 00:00:00
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pub_type: 杂志文章
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pub_type: 杂志文章
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更新日期:2005-10-01 00:00:00
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pub_type: 杂志文章
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