Earticle

초록

영어

A chitinolytic enzyme from the culture filtrates of Pseudomonas fluorescens was purified to apparent homogeneity and its kinetic properties were characterized. The molecular weight of the purified enzyme (NagA) was estimated by SDS–PAGE to be approximately 50 kDa. The optimum pH, temperature, and pH stability of NagA on synthetic substrate pNP-GlcNAc were determined to be pH 6.5, 37oC and pH 6–9, respectively. Its kinetic parameters on pNP-GlcNAc and pNP-(GlcNAc)2 were Km = 0.13 mM and 0.82 mM, and Vmax = 245 and 40 pmol/㎍/min, respectively. Chitinolytic activity of the purified NagA toward natural substrates (GlcNAc)n, n=2-5 was also determined by high performance anion-exchange chromatography with pulsed electrochemical detection (HPAEC-PED). The results suggest that NagA is an exo-type β-N-acetylglucosaminidase yielding GlcNAc as the final product from the chitooligosaccharides. Taken together, this is the first report of an exo-type chitinolytic enzyme based on the comparison of its peptide sequence from other chitinolytic enzyme produced by other microorganisms.

키워드

저자

• Ju Hee Ko [ Dept. of Biotechnology and The Biomaterial Engineering Research Center, The Catholic University of Korea, ]
• Jae Kweon Park [ Dept. of Biotechnology and The Biomaterial Engineering Research Center, The Catholic University of Korea, ]
• Woo Jung Kim [ Dept. of Biotechnology and The Biomaterial Engineering Research Center, The Catholic University of Korea, ]
• Hang Soo Jo [ Dept. of Biotechnology and The Biomaterial Engineering Research Center, The Catholic University of Korea, ]
• Yong Il Park [ Dept. of Biotechnology and The Biomaterial Engineering Research Center, The Catholic University of Korea, ]

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  한국당과학회 학술대회

• 간기

  연간

• 수록기간

  2006~2022

• 십진분류

  KDC 517 DDC 614