Preliminary characterization of a novel [beta]-agarase from Thalassospira profundimonas

Background The objective of this study was to characterize the agarase from a newly isolated agarolytic bacterium Thalassospira profundimaris fst-13007. Results Agarase-fst was purified to homogeneity which apparent molecular weight was 66.2 kDa. Its activity was optimal at 45 °C and pH 8 and was st...

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Bibliographic Details
Published in:SpringerPlus 2016-07, Vol.5 (1), p.1
Main Authors: Zeng, Cheng, Zhang, Longtao, Miao, Song, Zhang, Yi, Zeng, Shaoxiao, Zheng, Baodong
Format: Article
Language:English
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Summary:Background The objective of this study was to characterize the agarase from a newly isolated agarolytic bacterium Thalassospira profundimaris fst-13007. Results Agarase-fst was purified to homogeneity which apparent molecular weight was 66.2 kDa. Its activity was optimal at 45 °C and pH 8 and was stable at pH 5-9 or 30-50 °C. Agarase-fst required Mn2+ for agarase activity and inhibition by Cu2+, Fe3+ and EDTA. Tests of hydrolysis pattern and substrate specificity, TLC analysis and mass spectrometry of the hydrolysis products revealed that it is an endo-type [beta]-agarase hydrolyzing agarose into neoagarobiose, neoagarotetraose and neoagarohexaose. Results of MALDI-TOF-TOF/MS indicate that it lack of homology to previously identified proteins and present conserved domain of [beta]-agarase. Conclusion Agarase-fst from T. profundimaris fst-13007 was confirmed to be a novel endo-type [beta]-agarase.
ISSN:2193-1801
DOI:10.1186/s40064-016-2748-6