Purification and Characterization of a New Alginate Lyase from Marine Bacterium Vibrio Sp. SY08

Overview

Journal Mar Drugs

Publisher MDPI

Specialties Biology
Pharmacology

Date 2016 Dec 28

PMID 28025527

Citations 17

Authors

Shangyong Li

Linna Wang

Jianhua Hao

Mengxin Xing

Jingjing Sun

Mi Sun

Affiliations

Soon will be listed here.

Abstract

Unsaturated alginate disaccharides (UADs), enzymatically derived from the degradation of alginate polymers, are considered powerful antioxidants. In this study, a new high UAD-producing alginate lyase, AlySY08, has been purified from the marine bacterium sp. SY08. AlySY08, with a molecular weight of about 33 kDa and a specific activity of 1070.2 U/mg, showed the highest activity at 40 °C in phosphate buffer at pH 7.6. The enzyme was stable over a broad pH range (6.0-9.0) and retained about 75% activity after incubation at 40 °C for 2 h. Moreover, the enzyme was active in the absence of salt ions and its activity was enhanced by the addition of NaCl and KCl. AlySY08 resulted in an endo-type alginate lyase that degrades both polyM and polyG blocks, yielding UADs as the main product (81.4% of total products). All these features made AlySY08 a promising candidate for industrial applications in the production of antioxidants from alginate polysaccharides.

Citing Articles

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Efficient Degradation of Alginate and Preparation of Alginate Oligosaccharides by a Novel Biofunctional Alginate Lyase with High Activity and Excellent Thermophilic Features.

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