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논문 기본 정보

자료유형
학술저널
저자정보
Wang Lu (Department of Pathogen Biology College of Basic Medical Science Chongqing Medical University Chongqing 400016 P.R. China) Liu Qianqian (Department of Pathogen Biology College of Basic Medical Science Chongqing Medical University Chongqing 400016 P.R. China) Gong Xue (Department of Pathogen Biology College of Basic Medical Science Chongqing Medical University Chongqing 400016 P.R. China) Jian Wenwen (Department of Pathogen Biology College of Basic Medical Science Chongqing Medical University Chongqing 400016 P.R. China) Cui Yihong (Department of Pathogen Biology College of Basic Medical Science Chongqing Medical University Chongqing 400016 P.R. China) Jia Qianying (Department of Infectious Diseases The First Affiliated Hospital of Chongqing Medical University Chongqing 400016 P.R. China) Zhang Jibei (International Medical College Chongqing Medical University Chongqing 400016 P.R. China) Zhang Yi (International Medical College Chongqing Medical University Chongqing 400016 P.R. China) Guo Yanan (Department of Pathogen Biology College of Basic Medical Science Chongqing Medical University Chongqing 400016 P.R. China) Lu He (Department of Pathogen Biology College of Basic Medical Science Chongqing Medical University Chongqing 400016 P.R. China) Tu Zeng (Department of Pathogen Biology College of Basic Medical Science Chongqing Medical University Chongqing 400016 P.R. China)
저널정보
한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제33권 제2호
발행연도
2023.2
수록면
235 - 241 (7page)
DOI
10.4014/jmb.2209.09036

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Hyaluronidase (HAase) can enhance drug diffusion and dissipate edema by degrading hyaluronic acid (HA) in the extracellular matrix into unsaturated HA oligosaccharides in mammalian tissues. Microorganisms are recognized as valuable sources of HAase. In this study, a new hyaluronate lyase (HAaseD) from Bacillus sp. CQMU-D was expressed in Escherichia coli BL21, purified, and characterized. The results showed that HAaseD belonged to the polysaccharide lyase (PL) 8 family and had a molecular weight of 123 kDa. HAaseD could degrade chondroitin sulfate (CS) -A, CS-B, CSC, and HA, with the highest activity toward HA. The optimum temperature and pH value of HAaseD were 40°C and 7.0, respectively. In addition, HAaseD retained stability in an alkaline environment and displayed higher activity with appropriate concentrations of metal ions. Moreover, HAaseD was an endolytic hyaluronate lyase that could degrade HA to produce unsaturated HA oligosaccharides. Together, our findings indicate that HAaseD from Bacillus sp. CQMU-D is a new hyaluronate lyase and with excellent potential for application in industrial production.

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