4.7 Article

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

Journal

MARINE DRUGS
Volume 20, Issue 1, Pages -

Publisher

MDPI
DOI: 10.3390/md20010002

Keywords

beta-agarase; glycoside hydrolase family 16; neoagaro-oligosaccharide; partial hydrolytic product; hyaluronidase inhibition; Gilvimarinus agarilyticus JEA5

Funding

  1. Korea Institute of Ocean Science and Technology [PE99922]
  2. Korea Institute of Marine Science & Technology Promotion (KIMST) [PE99922] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)

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A new beta-agarase, Gaa16B, was identified and characterized for its activity and stability in agarose hydrolysis. The study also found that the partial hydrolysis products of Gaa16B exhibited high inhibition activity against hyaluronidase.
We recently identified a beta-agarase, Gaa16B, in the marine bacterium Gilvimarinus agarilyticus JEA5. Gaa16B, belonging to the glycoside hydrolase 16 family of beta-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 & DEG;C and pH 6-7, respectively, and the protein was highly stable at 55 & DEG;C for 90 min. Additionally, rGaa16Bc activity was strongly enhanced (2.3-fold) in the presence of 2.5 mM MnCl2. The K-m and V-max 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.

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