Molecular cloning and characterization of two β-agarases from marine bacterium Gilvimarinus agarilyticus JEA5

Title
Molecular cloning and characterization of two β-agarases from marine bacterium Gilvimarinus agarilyticus JEA5
Author(s)
이영득; 조은영; 박건후; 이수진; 허수진; 강도형; 오철홍
KIOST Author(s)
Lee, Youngdeuk(이영득)Jo, Eunyoung(조은영)Heo, Soo Jin(허수진)Kang, Do-Hyung(강도형)Oh, Chulhong(오철홍)
Publication Year
2016-11-25
Abstract
Agar is an important polysaccharide that consists of agarose and agaropectin. Agarose has a linear chain structure of alternating residues of 3-O-linked β-D-galactopyranose and 4-O-linked 3,6-anhydro-α-L-galactopyranose. Agarose is widely used in food, cosmetics and biological research. They are classified into α-agarase (EC. 3.2.1.158) and β-agarase (E.C. 2.2.1.81) according to the cleavage pattern. β-agarases have mainly classified into three GH families, i.e., GH-16, GH50, GH86 and 118. GH-16 family has most abundant members, including agarase, carrageenase, glucanase, galctosidase, laminarinase. We isolated the agar-degrading bacteria G. agarilyticus JEA5 from the coastal area of Jeju Island, Republic of Korea. The draft genome sequence (coverage 399×) of the JEA5 strain was obtained by paired-end sequencing on an Illumina High-Seq 2000 instrument at the Macrogen (Republic of Korea). Putative agarases were identified by the Basic Local Alignment Search Tool (BLAST) algorithm.We identified two GH-16 agarases and designated Gaa16A and Gaa16B. The Gaa16a has a 1323 bp of open reading frame (ORF), which encodes 441 amino acids. The predicted molecular mass and isoelectric point were 49 kDa and 4.9, respectively. A signal sequence is located in the N-terminal region. The conserved glycosyl hydrolase (GH) 16 and RICIN domain were identified in the poly peptide chain. Gaa16A showed optimal activity at 50°C and used in food, cosmetics and biological research. They are classified into α-agarase (EC. 3.2.1.158) and β-agarase (E.C. 2.2.1.81) according to the cleavage pattern. β-agarases have mainly classified into three GH families, i.e., GH-16, GH50, GH86 and 118. GH-16 family has most abundant members, including agarase, carrageenase, glucanase, galctosidase, laminarinase. We isolated the agar-degrading bacteria G. agarilyticus JEA5 from the coastal area of Jeju Island, Republic of Korea. The draft genome sequence (coverage 399×) of the JEA5 strain was obtained by paired-end sequencing on an Illumina High-Seq 2000 instrument at the Macrogen (Republic of Korea). Putative agarases were identified by the Basic Local Alignment Search Tool (BLAST) algorithm.We identified two GH-16 agarases and designated Gaa16A and Gaa16B. The Gaa16a has a 1323 bp of open reading frame (ORF), which encodes 441 amino acids. The predicted molecular mass and isoelectric point were 49 kDa and 4.9, respectively. A signal sequence is located in the N-terminal region. The conserved glycosyl hydrolase (GH) 16 and RICIN domain were identified in the poly peptide chain. Gaa16A showed optimal activity at 50°C and
URI
https://sciwatch.kiost.ac.kr/handle/2020.kiost/24289
Bibliographic Citation
The 12th KSMB Annual Meeting and Symposium, 2016, pp.208, 2016
Publisher
The 12th KSMB Annual Meeting and Symposium, 2016
Type
Conference
Language
English
Publisher
The 12th KSMB Annual Meeting and Symposium, 2016
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