Cloning, purification and biochemical characterization of beta agarase from the marine bacterium Pseudoalteromonas sp AG4 SCIE SCOPUS

Cited 48 time in WEB OF SCIENCE Cited 49 time in Scopus
Title
Cloning, purification and biochemical characterization of beta agarase from the marine bacterium Pseudoalteromonas sp AG4
Author(s)
Oh, Chulhong; Nikapitiya, Chamilani; Lee, Youngdeuk; Whang, Ilson; Kim, Se-Jae; Kang, Do-Hyung; Lee, Jehee
KIOST Author(s)
Kang, Do Hyung(강도형)
Publication Year
2010-05
Abstract
A gene (agrP) encoding a beta-agarase from Pseudoalteromonas sp. AG4 was cloned and expressed in Escherichia coli. The agrP primary structure consists of an 870-bp open reading frame (ORF) encoding 290 amino acids (aa). The predicted molecular mass and isoelectric point were determined at 33 kDa and 5.9, respectively. The signal peptide was predicted to be 21 aa. The deduced aa sequence showed 98.6% identity to beta-agarase from Pseudoalteromonas atlantica. The recombinant protein was purified as a fusion protein and biochemically characterized. The purified beta-agarase (AgaP) had specific activity of 204.4 and 207.5 units/mg towards agar and agarose, respectively. The enzyme showed maximum activity at 55A degrees C and pH 5.5. It was stable at pH 4.5 to 8.0 and below 55A degrees C for 1 h. The enzyme produced neoagarohexaose and neoagarotetraose from agar and in addition to that neoagarobiose from the agarose. The neoagarooligosaccharides were biologically active. Hence, AgaP is a useful enzyme source for use by cosmetic and pharmaceutical industries.
ISSN
1367-5435
URI
https://sciwatch.kiost.ac.kr/handle/2020.kiost/4100
DOI
10.1007/s10295-010-0694-9
Bibliographic Citation
JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY, v.37, no.5, pp.483 - 494, 2010
Publisher
SPRINGER HEIDELBERG
Subject
DEEP-SEA MICROBULBIFER; AMINO-ACID-SEQUENCES; EXTRACELLULAR-AGARASE; ENZYMATIC-PROPERTIES; PSEUDOMONAS-ATLANTICA; RECOMBINANT ENZYME; BACILLUS-SUBTILIS; ALPHA-AGARASE; STRAIN GJ1B; GENE
Keywords
Beta agarase; GHF-16; Neoagarooligosaccharides; Pseudoalteromonas spp.
Type
Article
Language
English
Document Type
Article
Publisher
SPRINGER HEIDELBERG
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