A Novel Agarase, Gaa16B, Isolated from the Marine Bacterium Gilvimarinus agarilyticus JEA5, and the Moisturizing Effect of Its Partial Hydrolysis Products SCIE SCOPUS

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Title
A Novel Agarase, Gaa16B, Isolated from the Marine Bacterium Gilvimarinus agarilyticus JEA5, and the Moisturizing Effect of Its Partial Hydrolysis Products
Author(s)
Lee, Young Deuk; Jo, Eunyoung; Lee, Yeon Ju; Eom, Tae Yang; Gang, Ye Hui; Kang, Yoon Hyeok; Marasinghe, Svini Dileepa; Hettiarachchi, Sachithra Amarin; Kang, Do Hyung; Oh, Chul Hong
KIOST Author(s)
Lee, Young Deuk(이영득)Jo, Eunyoung(조은영)Lee, Yeon Ju(이연주)Eom, Tae Yang(엄태양)Gang, Ye Hui(강예희)Marasinghe, Svini Dileepa(Svini)Kang, Do Hyung(강도형)Oh, Chul Hong(오철홍)
Alternative Author(s)
이영득; 조은영; 이연주; 엄태양; 강예희; 강윤혁; Svini; Amarin; 강도형; 오철홍
Publication Year
2022-01
Abstract
We recently identified a β-agarase, Gaa16B, in the marine bacterium Gilvimarinus agarilyticus JEA5. Gaa16B, belonging to the glycoside hydrolase 16 family of β-agarases, shows less than 70.9% amino acid similarity with previously characterized agarases. Recombinant Gaa16B lacking the carbohydrate-binding region (rGaa16Bc) was overexpressed in Escherichia coli and purified. Activity assays revealed the optimal temperature and pH of rGaa16Bc to be 55 ∘C and pH 6–7, respectively, and the protein was highly stable at 55 ∘C for 90 min. Additionally, rGaa16Bc activity was strongly enhanced (2.3-fold) in the presence of 2.5 mM MnCl2. The Km and Vmax of rGaa16Bc for agarose were 6.4 mg/mL and 953 U/mg, respectively. Thin-layer chromatography analysis revealed that rGaa16Bc can hydrolyze agarose into neoagarotetraose and neoagarobiose. Partial hydrolysis products (PHPs) of rGaa16Bc had an average molecular weight of 88–102 kDa and exhibited > 60% hyaluronidase inhibition activity at a concentration of 1 mg/mL, whereas the completely hydrolyzed product (CHP) showed no hyaluronidase at the same concentration. The biochemical properties of Gaa16B suggest that it could be useful for producing functional neoagaro-oligosaccharides. Additionally, the PHP of rGaa16Bc may be useful in promoting its utilization, which is limited due to the gel strength of agar.
ISSN
1660-3397
URI
https://sciwatch.kiost.ac.kr/handle/2020.kiost/41979
DOI
10.3390/md20010002
Bibliographic Citation
Marine Drugs, v.20, no.1, 2022
Publisher
Multidisciplinary Digital Publishing Institute (MDPI)
Keywords
β-agarase; glycoside hydrolase family 16; neoagaro-oligosaccharide; partial hydrolytic product; hyaluronidase inhibition; Gilvimarinus agarilyticus JEA5
Type
Article
Language
English
Document Type
Article
Publisher
Multidisciplinary Digital Publishing Institute (MDPI)
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