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Penicillium sp. Y6으로부터 chitosanase의 정제 및 특성규명 원문보기
Purification and characterization of the chitosanase from penicillium sp. Y6

  • 저자

    양주석

  • 학위수여기관

    慶尙大學校 大學院

  • 학위구분

    국내석사

  • 학과

    응용생명과학부

  • 지도교수

  • 발행년도

    2004

  • 총페이지

    viii, 42p.

  • 키워드

    Penicillium Y6 응용생명과학 생물학;

  • 언어

    kor

  • 원문 URL

    http://www.riss.kr/link?id=T10062167&outLink=K  

  • 초록

    A mold secreting chitosanases was isolated from soil and identified as a Penicillium species. The isolate, Penicillium sp Y6. secreted more chitosanase on CD-chitosan(0.25%) as a carbon source than on media with other carbon sources. This result indicates that the production of chitosanolytic enzyme was induced by chitosan. Furthermore, the chitosanase activity on a medium containing CD-chitosan plus yeast extract (0.5%) and peptone (0.5%) as the nitrogen sources was 4-fold higher than on media containing only that on CD-chitosan. This trait is highly desirable for large-scale production of chitosanase for industrial use. One of the chitosan-degrading enzymes was purified to homogeneity by ammonium sulfate precipitation followed by cation- exchange and gel filtration chromatographies. The enzyme was monomeric, and its molecular mass was estimated tobe 65 kDa. The optimum pH and temperature of the enzyme were 5.0 and 40℃, respectively. The activity was stable in the pH range 4 to 6.5 and at a temperature below 40℃. In the present study , one of the chitosan-degrading enzymes was purified, characterized, and then determined to be exo-type an chitosanase, by the viscometric assay and TLC analysis of the hydrolysate.


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