甲基弯菌IMV3011生物催化合成聚β-羟基丁酸酯途径中关键作用酶的活性(英文)

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	甲基弯菌IMV3011生物催化合成聚β-羟基丁酸酯途径中关键作用酶的活性(英文)
	Song H(宋昊)1,2 ; Zhang YX(张颖鑫)1,3; Kong WB(孔维宝)1,2; Xia CG(夏春谷)1
刊名	催化学报
	2012
卷号	33 期号:11 页码:1754-1761
关键词	enzyme activity biocatalysis poly-3-hydroxybutyrate methanotrophic bacteria 酶活性生物催化聚β-羟基丁酸酯甲烷氧化细菌
ISSN号	0253-9837
通讯作者	夏春谷
中文摘要	研究了甲烷单加氧酶(MMO)、β-酮硫解酶、乙酰乙酰CoA还原酶、聚β-羟基丁酸酯(PHB)合成酶及PHB降解酶在甲烷氧化细菌胞内PHB合成途径中的催化作用. 结果表明, MMO的活性随着胞内PHB的积累而持续下降, 而胞内高含量的PHB有助于减缓MMO活性的降低.β-酮硫解酶控制着反应体系进入PHB循环的入口, 在它和乙酰乙酰CoA还原酶的共同作用下, 生成聚合单体β-羟基丁酰, 二者活性在对数生长期达到峰值. PHB合成酶可将胞内的短链片段聚合, 形成具有稳定高分子量的长链聚酯; 当PHB合成酶活性最高时, 胞内PHB浓度也随之达到峰值. 同时, PHB降解酶活性随着PHB合成酶活性的增加而增加, 表明在PHB循环中, PHB的合成和降解实际上是同时发生的. PHB合成酶的活性基本决定了PHB的分子量, 但最终取决于PHB合成酶和PHB降解酶的共同作用.
英文摘要	The activities of the key enzymes involved in the intracellular poly-3-hydroxybutyrate (PHB) synthesis of Methylosinus trichosporium IMV3011 were studied under various cultivation conditions. The enzymes were methane monooxygenase (MMO), β-ketothiolase, acetoacetyl-CoA reductase, PHB synthetase, and PHB depolymerase. Each enzyme had a unique catalytic mechanism. MMO activity decreased continuously with PHB production, but PHB at a high concentration was beneficial for maintaining MMO activity because more NADH was released by PHB depolymerization. The important reaction for entering the PHB cycle was catalyzed by β-ketothiolase. The monomer of β-hydroxybutyrate was synthesized by the catalysis of β-ketothiolase and acetoacetyl-CoA reductase. PHB synthetase played an important role in the PHB synthesis routes. The activity of PHB synthetase increased with PHB production. The changes of enzyme activities involved in PHB synthetase and PHB depolymerase occurred together, which indicated that the polymerization and depolymerization of intracellular PHB occurred simultaneously. The molecular weight of PHB was determined mainly by the combined actions of PHB synthetase and PHB depolymerase. Some important intermediates in the tricarboxylic acid cycle were helpful for PHB production because they increased related enzyme activities in the PHB cycle.
学科主题	物理化学与绿色催化
收录类别	SCI
资助信息	the National Natural Science Foundation of China (21133011)
语种	英语
WOS记录号	WOS:000311882400002
公开日期	2013-10-11
内容类型	期刊论文
源URL	[http://210.77.64.217/handle/362003/3907]
专题	兰州化学物理研究所_OSSO国家重点实验室
作者单位	1.Chinese Acad Sci, Lanzhou Inst Chem Phys, State Key Lab Oxo Synth & Select Oxidat, Lanzhou 730000, Gansu, Peoples R China 2.Chinese Acad Sci, Grad Univ, Beijing 100049, Peoples R China 3.Chinese Acad Sci, Ningbo Inst Mat Technol & Engn, Div Funct Mat & Nanodevices, Ningbo 315201, Zhejiang, Peoples R China
推荐引用方式 GB/T 7714	Song H(宋昊),Zhang YX(张颖鑫),Kong WB(孔维宝),等. 甲基弯菌IMV3011生物催化合成聚β-羟基丁酸酯途径中关键作用酶的活性(英文)[J]. 催化学报,2012,33(11):1754-1761.
APA	Song H,Zhang YX,Kong WB,&Xia CG.(2012).甲基弯菌IMV3011生物催化合成聚β-羟基丁酸酯途径中关键作用酶的活性(英文).催化学报,33(11),1754-1761.
MLA	Song H,et al."甲基弯菌IMV3011生物催化合成聚β-羟基丁酸酯途径中关键作用酶的活性(英文)".催化学报 33.11(2012):1754-1761.