Production of a thermo-tolerant kappa-carrageenase via a food-grade host and anti-oxidant activity of its enzymatic hydrolysate
- Authors
- Li, Shangyong; He, Ningning; Han, Qi; Li, Xiao; Jung, Samil; Lee, Beom Suk; Mongre, Raj Kumar; Wang, Zhi-Peng; Wang, Linna; Lee, Myeong-Sok
- Issue Date
- 1-Mar-2021
- Publisher
- ELSEVIER SCI LTD
- Keywords
- Anti-oxidant activity; Thermo-tolerance; κ-Carradiaose; κ-Carrageenase
- Citation
- FOOD CHEMISTRY, v.339, pp 1 - 9
- Pages
- 9
- Journal Title
- FOOD CHEMISTRY
- Volume
- 339
- Start Page
- 1
- End Page
- 9
- URI
- https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/840
- DOI
- 10.1016/j.foodchem.2020.128027
- ISSN
- 0308-8146
1873-7072
- Abstract
- kappa-Carrageenase cleaves the beta-(1-4) linkages of kappa-carrageenan into kappa-carrageenan oligosaccharides (kappa-COS), which exhibit various biological activities. In this study, a glycoside hydrolase (GH) family 16 kappa-carrageenase gene, cgkA, was cloned from the marine bacterium Vibrio sp. SY01 and secretory expressed in a food-grade host, Yarrowia lipolytica. The specific activity of the purified CgkA was 12.5 U/mg. Determination of biochemical properties showed that CgkA was a thermo-tolerant enzyme, and 59.9% of the initial enzyme activity was recovered by immediately placing the sample at 20 degrees C for 30 min after enzymatic inactivation by boiling for 5 min. The recombinant CgkA was an endo-type enzyme, the main enzymatic product was kappa-carradiaose (accounting for 87.6% of total products), and kappa-carratetraose was the minimum substrate. Additionally, in vitro and in vivo analyses indicated that enzymatic kappa-carradiaose possesses anti-oxidant activity. These features make CgkA as a promising candidate for biotechnological applications in the production of anti-oxidant kappa-COS.
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