期刊
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
卷 86, 期 -, 页码 525-534出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.ijbiomac.2016.01.106
关键词
Stenotrophomonas sp; Agarase; Characterization; Enzymatic hydrolysates; Antioxidant activity
资金
- National Natural Science Foundation of China [31401632]
- Projects of Xiamen Southern Ocean Technology Center of China [13PZP002NF03, 13GZP004NF10]
An extracellular agarase from marine bacterium Stenotrophomonas sp. NTa was purified to homogeneity. By size exclusion chromatography and SDS-PAGE analysis, the enzyme was determined to be a homodimer with monomeric molecular mass of 89.0 kDa. The optimal temperature and pH of strain NTa agarase were 40 degrees C and 10.0, respectively. It exhibited striking stability across a wide pH range of 5.0-11.0. Agarase from Stenotrophomonas sp. NTa had a relatively good resistance against the detected inhibitors, detergents and urea denaturant. The K-m and V-max for agar were 11.3 mg/ml and 25.4 U/mg, respectively. Thin layer chromatography analysis, mass spectrometry, and enzyme assay using p-nitrophenyl-alpha/beta-D-galactopyranoside revealed that strain NTa agarase was a beta-agarase that degraded agarose into neoagarobiose, neoagarotetraose and neoagarohexaose as the predominant products, as well as a small amount of 3,6-anhydro-alpha-L-galactose. This is the first to present evidence of agarolytic activity in strain from genus Stenotrophomonas. (C) 2016 Published by Elsevier B.V.
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