%0 Journal Article
%T Investigation on Enzymatic Synthesis of L-Theanine with Zinc(Ⅱ)-L-Glutamine Complex and Its Mechanism<br>以L-谷氨酰胺—锌(Ⅱ)配合物为供体酶法制备茶氨酸及其反应机理
%A HU Guo-mei
%A YAO Zhong
%A WANG Hao-qi
%A ZHOU Zhi
%A XIONG Qiang
%A XU Hong
%A WEI Ping
%A <br>胡国梅
%A 姚忠
%A 王浩琦
%A 周治
%A 熊强
%A 徐虹
%A 韦萍
%J 过程工程学报
%D 2012
%I 
%X To restrain the side reaction of autotranspeptidation, the complex of L-glutamine-Zn(Ⅱ) Zn(Gln)2] was prepared and used for enzymatic synthesis of theanine via γ-glutamyltranspeptidation (GGT) reaction. The stability and reactivity of Zn(Gln)2 were satisfactory under the reaction conditions. Moreover, autotranspeptidation was restrained effectively when Zn(Gln)2 instead of L-glutamine (Gln) was used as the γ-glutamyl donor. The kinetic parameter Km of B. subtillus GGT toward Zn(Gln)2 and Gln was calculated to be 0.53 and 1.01 mmol/L respectively. Under the conditions of 6 mmol/L Zn(Gln)2, 200 mmol/L ethylamine, and 0.5 U/mL GGT, 7.38 mmol/L of theanine was obtained after incubation at 37℃ for 2 h, indicating an increase of 14.42% compared with that using Gln as the donor substrate.
%K L-theanine
%K γ-glutamyltranspeptidase
%K Zn(Ⅱ)-L-glutamine
%K enzymatic synthesis
%K autotranspeptidation<br>L-茶氨酸
%K γ-谷氨酰转肽酶
%K L-谷氨酰胺-锌(Ⅱ)配合物
%K 酶法合成
%K 自转肽
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=5B3AB970F71A803DEACDC0559115BFCF0A068CD97DD29835&cid=3FCF8B1A330466D5&jid=B9EE12934D19905403D996AE65CEEEED&aid=B39D47F72CB13A768BDE61D2090650DD&yid=99E9153A83D4CB11&vid=59906B3B2830C2C5&iid=0B39A22176CE99FB&sid=E2B9962CCD971A0D&eid=EBD6B792C9111B87&journal_id=1009-606X&journal_name=过程工程学报&referenced_num=0&reference_num=0