Variation in copolymer composition and molecular weight of polyhydroxyalkanoate generated by saturation mutagenesis of Aeromonas caviae PHA synthase.

Variation in copolymer composition and molecular weight of polyhydroxyalkanoate generated by saturation mutagenesis of Aeromonas caviae PHA synthase.
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DOI:
10.1002/mabi.200700023
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发表时间:
2007-06
影响因子:
4.6
通讯作者:
Takeharu Tsuge;Shinko Watanabe;Shun Sato;T. Hiraishi;H. Abe;Y. Doi;S. Taguchi
Takeharu Tsuge;Shinko Watanabe;Shun Sato;T. Hiraishi;H. Abe;Y. Doi;S. Taguchi
中科院分区:
工程技术3区
文献类型:
--
作者:
Takeharu Tsuge;Shinko Watanabe;Shun Sato;T. Hiraishi;H. Abe;Y. Doi;S. Taguchi

文献摘要

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聚羟基脂肪酸酯 (PHA) 合酶活性位点组氨酸下游两个残基的氨基酸取代可有效改变 PHA 的组成和分子量。在本研究中,对来自豚鼠气单胞菌的PHA合酶(PhaCAc)应用Ala505位点的饱和诱变,以研究其对真养罗尔斯通氏菌合成的PHA的组成和分子量的影响。 PHA 的共聚物组成和分子量因氨基酸取代而异。共聚物组成与细胞的 PHA 合酶活性之间存在密切关系。这一发现将作为生产定制 PHA 的基本原理。
Amino acid substitutions at two residues downstream from the active-site histidine of polyhydroxyalkanoate (PHA) synthases are effective for changing the composition and the molecular weight of PHA. In this study, saturation mutagenesis at the position Ala505 was applied to PHA synthase (PhaCAc) from Aeromonas caviae to investigate the effects on the composition and the molecular weight of PHA synthesized in Ralstonia eutropha. The copolymer composition and molecular weight of PHA were varied by association with amino acid substitutions. There was a strong relationship between copolymer composition and PHA synthase activity of the cells. This finding will serve as a rationale for producing tailor-made PHAs.