高校化学工程学报
高校化學工程學報
고교화학공정학보
JOURNAL OF CHEMICAL ENGINEERING OF CHINESE UNIVERSITIES
2013年
2期
339-343
,共5页
类红球菌羧酸酯酶%有机溶剂%转酯反应%手性选择性
類紅毬菌羧痠酯酶%有機溶劑%轉酯反應%手性選擇性
류홍구균최산지매%유궤용제%전지반응%수성선택성
Rhodobacter sphaeroides carboxyl esterase%organic solvent%transesterification%enantioselectivity
以来源于类红球细菌(Rhodobacter sphaeroides)的羧酸酯酶 RspE 为催化剂,首次探讨了它在有机溶剂中的催化特性,并在研究中将1-苯乙醇与乙酸乙烯酯的转酯反应作为模型反应.比较5种不同有机溶剂以及4个不同温度对酯酶RspE催化反应的影响,发现在45oC乙腈作为溶剂时酶的催化活性最高.而在酶的稳定性研究中,发现酯酶RspE在有机溶剂中暴露4天后,催化转酯反应进行两天的保留活性为58.3%,表明有机溶剂中的长时间暴露使得酯酶的催化活性有损失.在最适条件下反应6天后的结果显示,转化率达到了47.9%,而对映体选择性值达到了64,表明该羧酸酯酶对1-R-苯乙醇具有良好的手性选择性.经本实验研究发现,类红球细菌羧酸酯酶 RspE 在有机溶剂中能够有选择性地催化1-苯乙醇转酯反应的进行,表明该酯酶不但可以在水相中催化水解反应的进行,还可以作为一种新的生物催化剂应用于有机相催化工业.
以來源于類紅毬細菌(Rhodobacter sphaeroides)的羧痠酯酶 RspE 為催化劑,首次探討瞭它在有機溶劑中的催化特性,併在研究中將1-苯乙醇與乙痠乙烯酯的轉酯反應作為模型反應.比較5種不同有機溶劑以及4箇不同溫度對酯酶RspE催化反應的影響,髮現在45oC乙腈作為溶劑時酶的催化活性最高.而在酶的穩定性研究中,髮現酯酶RspE在有機溶劑中暴露4天後,催化轉酯反應進行兩天的保留活性為58.3%,錶明有機溶劑中的長時間暴露使得酯酶的催化活性有損失.在最適條件下反應6天後的結果顯示,轉化率達到瞭47.9%,而對映體選擇性值達到瞭64,錶明該羧痠酯酶對1-R-苯乙醇具有良好的手性選擇性.經本實驗研究髮現,類紅毬細菌羧痠酯酶 RspE 在有機溶劑中能夠有選擇性地催化1-苯乙醇轉酯反應的進行,錶明該酯酶不但可以在水相中催化水解反應的進行,還可以作為一種新的生物催化劑應用于有機相催化工業.
이래원우류홍구세균(Rhodobacter sphaeroides)적최산지매 RspE 위최화제,수차탐토료타재유궤용제중적최화특성,병재연구중장1-분을순여을산을희지적전지반응작위모형반응.비교5충불동유궤용제이급4개불동온도대지매RspE최화반응적영향,발현재45oC을정작위용제시매적최화활성최고.이재매적은정성연구중,발현지매RspE재유궤용제중폭로4천후,최화전지반응진행량천적보류활성위58.3%,표명유궤용제중적장시간폭로사득지매적최화활성유손실.재최괄조건하반응6천후적결과현시,전화솔체도료47.9%,이대영체선택성치체도료64,표명해최산지매대1-R-분을순구유량호적수성선택성.경본실험연구발현,류홍구세균최산지매 RspE 재유궤용제중능구유선택성지최화1-분을순전지반응적진행,표명해지매불단가이재수상중최화수해반응적진행,환가이작위일충신적생물최화제응용우유궤상최화공업.
In this study, a carboxyl esterase from Rhodobacter sphaeroides was introduced as a catalyst in organic solvent, and the transesterification of 1-phenethyl alcohol and vinyl acetate was served as a model reaction. It was found that changes in used solvent and temperature influence the activity of the esterase and it was observed that the highest activity was obtained when acetonitrile was served as the solvent with the catalytic temperature of 45℃. However, after four days’ exposure in organic solvent, the relative activity of the esterase decreases to 58.3%, which indicates that the esterase is partially denatured due to the toxicity of organic solvent. Six days’ reaction carried out in optimal condition shows that the molar conversation reaches to 47.9%and the E value is 64. It demonstrated that this carboxyl esterase displays high enantioselectivity toward R-1-phenetyl alcohol and can be applied to industrial manufacturing as a novel biocatalyst.