A Novel Glycosyl Hydrolase Family 16 beta-Agarase from the Agar-Utilizing Marine Bacterium Gilvimarinus agarilyticus JEA5: the First Molecular and Biochemical Characterization of Agarase in Genus Gilvimarinus SCIE SCOPUS KCI

Cited 2 time in WEB OF SCIENCE Cited 3 time in Scopus
Title
A Novel Glycosyl Hydrolase Family 16 beta-Agarase from the Agar-Utilizing Marine Bacterium Gilvimarinus agarilyticus JEA5: the First Molecular and Biochemical Characterization of Agarase in Genus Gilvimarinus
Author(s)
Lee, Youngdeuk; Jo, Eunyoung; Lee, Yeon-Ju; Hettiarachchi, Sachithra Amarin; Park, Gun-Hoo; Lee, Su-Jin; Heo, Soo-Jin; Kang, Do-Hyung; Oh, Chulhong
KIOST Author(s)
Lee, Young Deuk(이영득)Jo, Eun Young(조은영)Lee, Yeon Ju(이연주)Heo, Soo Jin(허수진)Kang, Do Hyung(강도형)Oh, Chul Hong(오철홍)
Publication Year
2018-05
Abstract
The agarase gene gaa16a was identified from a draft genome sequence of Gilvimarinus agarilyticus JEA5, an agar-utilizing marine bacterium. Recently, three agarase-producing bacteria, G. chinensis, G. polysaccharolyticus, and G. agarilyticus, in the genus Gilvimarinus were reported. However, there have been no reports of the molecular characteristics and biochemical properties of these agarases. In this study, we analyzed the molecular characteristics and biochemical properties of agarases in Gilvimarinus. Gaa16A comprised a 1,323-bp open reading frame encoding 441 amino acids. The predicted molecular mass and isoelectric point were 49 kDa and 4.9, respectively. The amino acid sequence of Gaa16A showed features typical of glycosyl hydrolase family 16 (GH16) beta-agarases, including a GH16 domain, carbohydrate-binding region (RICIN domain), and signal peptide. Recombinant Gaa16A (excluding the signal peptide and carbohydrate-binding region, rGaa16A) was expressed as a fused protein with maltose-binding protein at its N-terminus in Escherichia coli. rGaa16A had maximum activity at 55 degrees C and pH 7.0 and 103 U/mg of specific activity in the presence of 2.5 mM CaCl2 . The enzyme hydrolyzed agarose to yield neoagarotetraose as the main product. This enzyme may be useful for industrial production of functional neoagaro-oligosaccharides.
ISSN
1017-7825
URI
https://sciwatch.kiost.ac.kr/handle/2020.kiost/926
DOI
10.4014/jmb.1709.09050
Bibliographic Citation
JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, v.28, no.5, pp.776 - 783, 2018
Publisher
KOREAN SOC MICROBIOLOGY & BIOTECHNOLOGY
Subject
PURIFICATION; CLONING; EXPRESSION; POLYSACCHARIDE; GALACTOSE; GENOME; ENZYME; SP.
Keywords
Gilvimarinus; agarase; neoagaro-oligosaccharides; cloning; overexpression
Type
Article
Language
English
Document Type
Article
Publisher
KOREAN SOC MICROBIOLOGY & BIOTECHNOLOGY
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