Purification and Characterization of a Novel Alginate Lyase from a Marine <i>Streptomyces</i> Species Isolated from Seaweed

Alginate, a natural polysaccharide derived from brown seaweed, is finding multiple applications in biomedicine via its transformation through chemical, physical, and, increasingly, enzymatic processes. In this study a novel alginate lyase, AlyDS44, was purified and characterized from a marine actino...

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Autores principales:	Thi Nhu Thuong Nguyen, Timothy Chataway, Ricardo Araujo, Munish Puri, Christopher Milton Mathew Franco
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	actinobacteria alginate lyase polysaccharide-degrading enzyme protein sequence bifunctional enzyme seaweed Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/f6727806606648388f10f9f249d21812
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spelling	oai:doaj.org-article:f6727806606648388f10f9f249d218122021-11-25T18:12:38ZPurification and Characterization of a Novel Alginate Lyase from a Marine <i>Streptomyces</i> Species Isolated from Seaweed10.3390/md191105901660-3397https://doaj.org/article/f6727806606648388f10f9f249d218122021-10-01T00:00:00Zhttps://www.mdpi.com/1660-3397/19/11/590https://doaj.org/toc/1660-3397Alginate, a natural polysaccharide derived from brown seaweed, is finding multiple applications in biomedicine via its transformation through chemical, physical, and, increasingly, enzymatic processes. In this study a novel alginate lyase, AlyDS44, was purified and characterized from a marine actinobacterium, <i>Streptomyces luridiscabiei</i>, which was isolated from decomposing seaweed. The purified enzyme had a specific activity of 108.6 U/mg, with a molecular weight of 28.6 kDa, and was composed of 260 amino acid residues. AlyDS44 is a bifunctional alginate lyase, active on both polyguluronate and polymannuronate, though it preferentially degrades polyguluronate. The optimal pH of this enzyme is 8.5 and the optimal temperature is 45 °C. It is a salt-tolerant alginate lyase with an optimal activity at 0.6 M NaCl. Metal ions Mn<sup>2+</sup>, Co<sup>2+</sup>, and Fe<sup>2+</sup> increased the alginate degrading activity, but it was inhibited in the presence of Zn<sup>2+</sup> and Cu<sup>2+</sup>. The highly conserved regions of its amino acid sequences indicated that AlyDS44 belongs to the polysaccharide lyase family 7. The main breakdown products of the enzyme on alginate were disaccharides, trisaccharides, and tetrasaccharides, which demonstrated that this enzyme acted as an endo-type alginate lyase. AlyDS44 is a novel enzyme, with the potential for efficient production of alginate oligosaccharides with low degrees of polymerization.Thi Nhu Thuong NguyenTimothy ChatawayRicardo AraujoMunish PuriChristopher Milton Mathew FrancoMDPI AGarticleactinobacteriaalginate lyasepolysaccharide-degrading enzymeprotein sequencebifunctional enzymeseaweedBiology (General)QH301-705.5ENMarine Drugs, Vol 19, Iss 590, p 590 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	actinobacteria alginate lyase polysaccharide-degrading enzyme protein sequence bifunctional enzyme seaweed Biology (General) QH301-705.5
spellingShingle	actinobacteria alginate lyase polysaccharide-degrading enzyme protein sequence bifunctional enzyme seaweed Biology (General) QH301-705.5 Thi Nhu Thuong Nguyen Timothy Chataway Ricardo Araujo Munish Puri Christopher Milton Mathew Franco Purification and Characterization of a Novel Alginate Lyase from a Marine <i>Streptomyces</i> Species Isolated from Seaweed
description	Alginate, a natural polysaccharide derived from brown seaweed, is finding multiple applications in biomedicine via its transformation through chemical, physical, and, increasingly, enzymatic processes. In this study a novel alginate lyase, AlyDS44, was purified and characterized from a marine actinobacterium, <i>Streptomyces luridiscabiei</i>, which was isolated from decomposing seaweed. The purified enzyme had a specific activity of 108.6 U/mg, with a molecular weight of 28.6 kDa, and was composed of 260 amino acid residues. AlyDS44 is a bifunctional alginate lyase, active on both polyguluronate and polymannuronate, though it preferentially degrades polyguluronate. The optimal pH of this enzyme is 8.5 and the optimal temperature is 45 °C. It is a salt-tolerant alginate lyase with an optimal activity at 0.6 M NaCl. Metal ions Mn<sup>2+</sup>, Co<sup>2+</sup>, and Fe<sup>2+</sup> increased the alginate degrading activity, but it was inhibited in the presence of Zn<sup>2+</sup> and Cu<sup>2+</sup>. The highly conserved regions of its amino acid sequences indicated that AlyDS44 belongs to the polysaccharide lyase family 7. The main breakdown products of the enzyme on alginate were disaccharides, trisaccharides, and tetrasaccharides, which demonstrated that this enzyme acted as an endo-type alginate lyase. AlyDS44 is a novel enzyme, with the potential for efficient production of alginate oligosaccharides with low degrees of polymerization.
format	article
author	Thi Nhu Thuong Nguyen Timothy Chataway Ricardo Araujo Munish Puri Christopher Milton Mathew Franco
author_facet	Thi Nhu Thuong Nguyen Timothy Chataway Ricardo Araujo Munish Puri Christopher Milton Mathew Franco
author_sort	Thi Nhu Thuong Nguyen
title	Purification and Characterization of a Novel Alginate Lyase from a Marine <i>Streptomyces</i> Species Isolated from Seaweed
title_short	Purification and Characterization of a Novel Alginate Lyase from a Marine <i>Streptomyces</i> Species Isolated from Seaweed
title_full	Purification and Characterization of a Novel Alginate Lyase from a Marine <i>Streptomyces</i> Species Isolated from Seaweed
title_fullStr	Purification and Characterization of a Novel Alginate Lyase from a Marine <i>Streptomyces</i> Species Isolated from Seaweed
title_full_unstemmed	Purification and Characterization of a Novel Alginate Lyase from a Marine <i>Streptomyces</i> Species Isolated from Seaweed
title_sort	purification and characterization of a novel alginate lyase from a marine <i>streptomyces</i> species isolated from seaweed
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/f6727806606648388f10f9f249d21812
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Purification and Characterization of a Novel Alginate Lyase from a Marine <i>Streptomyces</i> Species Isolated from Seaweed

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