Isolation and characterization of a novel endoglucanase from a Bursaphelenchus xylophilus metagenomic library.

A novel gene (designated as cen219) encoding endoglucanase was isolated from a Bursaphelenchus xylophilus metagenomic library by functional screening. Sequence analysis revealed that cen219 encoded a protein of 367 amino acids. SDS-PAGE analysis of purified endoglucanase suggested that Cen219 was a...

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Autores principales:	Lin Zhang, Yongxin Fan, Haoying Zheng, Fengguang Du, Ke-qin Zhang, Xiaowei Huang, Linfeng Wang, Man Zhang, Qiuhong Niu
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/9eb196372dc04359a7501b230562ac81
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spelling	oai:doaj.org-article:9eb196372dc04359a7501b230562ac812021-11-18T08:40:12ZIsolation and characterization of a novel endoglucanase from a Bursaphelenchus xylophilus metagenomic library.1932-620310.1371/journal.pone.0082437https://doaj.org/article/9eb196372dc04359a7501b230562ac812013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24386096/?tool=EBIhttps://doaj.org/toc/1932-6203A novel gene (designated as cen219) encoding endoglucanase was isolated from a Bursaphelenchus xylophilus metagenomic library by functional screening. Sequence analysis revealed that cen219 encoded a protein of 367 amino acids. SDS-PAGE analysis of purified endoglucanase suggested that Cen219 was a monomeric enzyme with a molecular mass of 40 kDa. The optimum temperature and pH for endoglucanase activity of Cen219 was separately 50 °C and 6.0. It was stable from 30 to 50 °C, and from pH 4.0 to 7.0. The activity was significantly enhanced by Mn(2+) and dramatically reduced by detergent SDS and metals Fe(3+), Cu(2+) or Hg(2+). The enzyme hydrolyzed a wide range of β-1, 3-, and β-1, 4-linked polysaccharides, with varying activities. Activities towards microcrystalline cellulose and filter paper were relatively high, while the highest activity was towards oat gum. The Km and Vmax of Cen219 towards CMC was 17.37 mg/ml and 333.33 U/mg, respectively. The findings have an insight into understanding the molecular basis of host-parasite interactions in B. xylophilus species. The properties also make Cen219 an interesting enzyme for biotechnological application.Lin ZhangYongxin FanHaoying ZhengFengguang DuKe-qin ZhangXiaowei HuangLinfeng WangMan ZhangQiuhong NiuPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 12, p e82437 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Lin Zhang Yongxin Fan Haoying Zheng Fengguang Du Ke-qin Zhang Xiaowei Huang Linfeng Wang Man Zhang Qiuhong Niu Isolation and characterization of a novel endoglucanase from a Bursaphelenchus xylophilus metagenomic library.
description	A novel gene (designated as cen219) encoding endoglucanase was isolated from a Bursaphelenchus xylophilus metagenomic library by functional screening. Sequence analysis revealed that cen219 encoded a protein of 367 amino acids. SDS-PAGE analysis of purified endoglucanase suggested that Cen219 was a monomeric enzyme with a molecular mass of 40 kDa. The optimum temperature and pH for endoglucanase activity of Cen219 was separately 50 °C and 6.0. It was stable from 30 to 50 °C, and from pH 4.0 to 7.0. The activity was significantly enhanced by Mn(2+) and dramatically reduced by detergent SDS and metals Fe(3+), Cu(2+) or Hg(2+). The enzyme hydrolyzed a wide range of β-1, 3-, and β-1, 4-linked polysaccharides, with varying activities. Activities towards microcrystalline cellulose and filter paper were relatively high, while the highest activity was towards oat gum. The Km and Vmax of Cen219 towards CMC was 17.37 mg/ml and 333.33 U/mg, respectively. The findings have an insight into understanding the molecular basis of host-parasite interactions in B. xylophilus species. The properties also make Cen219 an interesting enzyme for biotechnological application.
format	article
author	Lin Zhang Yongxin Fan Haoying Zheng Fengguang Du Ke-qin Zhang Xiaowei Huang Linfeng Wang Man Zhang Qiuhong Niu
author_facet	Lin Zhang Yongxin Fan Haoying Zheng Fengguang Du Ke-qin Zhang Xiaowei Huang Linfeng Wang Man Zhang Qiuhong Niu
author_sort	Lin Zhang
title	Isolation and characterization of a novel endoglucanase from a Bursaphelenchus xylophilus metagenomic library.
title_short	Isolation and characterization of a novel endoglucanase from a Bursaphelenchus xylophilus metagenomic library.
title_full	Isolation and characterization of a novel endoglucanase from a Bursaphelenchus xylophilus metagenomic library.
title_fullStr	Isolation and characterization of a novel endoglucanase from a Bursaphelenchus xylophilus metagenomic library.
title_full_unstemmed	Isolation and characterization of a novel endoglucanase from a Bursaphelenchus xylophilus metagenomic library.
title_sort	isolation and characterization of a novel endoglucanase from a bursaphelenchus xylophilus metagenomic library.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/9eb196372dc04359a7501b230562ac81
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Isolation and characterization of a novel endoglucanase from a Bursaphelenchus xylophilus metagenomic library.

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