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Purification and characterization of poly(l-lactic acid)-degrading enzymes from Amycolatopsis orientalis ssp. orientalis.

Purification and characterization of poly(l-lactic acid)-degrading enzymes from Amycolatopsis orientalis ssp. orientalis. Research Abstract Details 

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  • Purification and characterization of poly(l-lactic acid)-degrading enzymes from Amycolatopsis orientalis ssp. orientalis. Abstract Text:

    fan liFan Li,sha wangSha Wang,weifeng liuWeifeng Liu,guanjun chenGuanjun Chen,

    Polylactide or poly(l-lactic acid) (PLA) is a commercially promising material for use as a renewable and biodegradable plastic. Three novel PLA-degrading enzymes, named PLAase I, II and III, were purified to homogeneity from the culture supernatant of an effective PLA-degrading bacterium, Amycolatopsis orientalis ssp. orientalis. The molecular masses of these three PLAases as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis were 24.0, 19.5 and 18.0 kDa, with the pH optima being 9.5, 10.5 and 9.5, respectively. The optimal temperature for the enzyme activities was 50-60 degrees C. All the purified enzymes could degrade high-molecular-weight PLA film as well as casein, and the PLA-degrading activities were strongly inhibited by serine protease inhibitors such as phenylmethylsulfonyl fluoride and aprotinin, but were not susceptive to chymostatin and pepstatin. Taken together, these data demonstrated that A. orientalis ssp. orientalis produces multiple serine-like proteases to utilize extracellular polylactide as a sole carbon source.

    Purification and characterization of poly(l-lactic acid)-degrading enzymes from Amycolatopsis orientalis ssp. orientalis. Publishing Authors By Initials

    f liF Li,s wangS Wang,w liuW Liu,g chenG Chen,

    For similar abstracts research abstracts see: abstracts research

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    Purification and characterization of poly(l-lactic acid)-degrading enzymes from Amycolatopsis orientalis ssp. orientalis. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: FEMS microbiology letters

    VOLUME: 282

    Page Numbers: 52-8

    Journal Abbreviation: FEMS Microbiol. Lett.

    ISSN: 0378-1097

    DAY: 18

    MONTH: 03

    YEAR: 2008

    Purification and characterization of poly(l-lactic acid)-degrading enzymes from Amycolatopsis orientalis ssp. orientalis. Information

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    LANGUAGE: eng

    NlmUniqueID: 7705721

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    Grant and Affiliation Information for Purification and characterization of poly(l-lactic acid)-degrading enzymes from Amycolatopsis orientalis ssp. orientalis.

    AFFILIATION: The State Key Laboratory of Microbial Technology, School of Life Science, Shandong University, Jinan, Shandong, China.

    Country: England

    England Research PublicationEngland Research Publication

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    MEDLINETA: FEMS Microbiol Lett

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