Abstract
An alginate lyase-producing bacterial strain, Vibrio sp. QY105, was isolated from sea mud of Qingdao. It secreted 90 % of total enzyme activity within the first 20 h of fermentation. An alginate lyase, AlyV5, with an apparent MW of 37 kDa and a specific activity of 2152 U/mg was purified from the culture supernatant. It was most active at 38 °C and pH 7.0 in 20 mM Tris/HCl. The enzyme was stable over a broad pH range (6.0–9.0) and retained ~40 % activity after holding at 90 °C for 10 min. AlyV5 showed activities towards both polyguluronate and polymannuronate, but degraded the former more efficiently. AlyV5 mainly produced disaccharide, trisaccharide and tetrasaccharide from polyguluronate, trisaccharide, tetrasaccharide and pentasaccharide from polymannuronate.
Purpose of work
The purpose of this study is to find a polyG-preference alginate lyase for the saccharification of alginate combined with our polyM-preference alginate lyases.
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Acknowledgments
We are very grateful to Dr. Guangli Yu and Dr. Xia Zhao (School of Medicine and Pharmacy, Ocean University of China, China) for the preparation of polyM and polyG. The research was supported by the National High-tech R&D Program of China (2011AA09070304) and Special Fund for Marine Scientific Research in the Public Interest (201105027-3).
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Wang, Y., Guo, EW., Yu, WG. et al. Purification and characterization of a new alginate lyase from a marine bacterium Vibrio sp.. Biotechnol Lett 35, 703–708 (2013). https://doi.org/10.1007/s10529-012-1134-x
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DOI: https://doi.org/10.1007/s10529-012-1134-x