The Role of a Tyrosine Residue of Bacterial Liquefying α-Amylase in the Enzymatic Hydrolysis of Linear Substrates as Studied by Chemical Modification with Acetic Anhydride*

1974 ◽  
Vol 76 (1) ◽  
pp. 7-13 ◽  
Author(s):  
Masatake OHNISHI ◽  
Toshihiko SUGANUMA ◽  
Keitaro HIROMI
2016 ◽  
Vol 199 ◽  
pp. 49-58 ◽  
Author(s):  
Shaoni Sun ◽  
Shaolong Sun ◽  
Xuefei Cao ◽  
Runcang Sun

1994 ◽  
Vol 72 (11) ◽  
pp. 2312-2317 ◽  
Author(s):  
Robert Chênevert ◽  
Michel Desjardins

We report two different chemoenzymatic enantioselective syntheses of baclofen based on the distinction between enantiotopic ester groups in compounds bearing a prochiral centre. In the first approach, the key step is the highly stereoselective enzymatic hydrolysis of dimethyl 3-(4-chlorophenyl)glutarate by chymotrypsin in an aqueous medium. In the second approach, the key step is the enzyme-catalyzed esterification of 2-(4-chloropheny 1)-1,3-propanediol by acetic anhydride in the presence of a lipase in an organic medium.


1959 ◽  
Vol 6 (2) ◽  
pp. 163-170 ◽  
Author(s):  
Russell J. Barrnett ◽  
George E. Palade

Experiments which combined histochemistry and electron microscopy were performed in studying the sites of enzymatic hydrolysis of thiolacetic acid in the presence of lead ions in diaphragmatic and cardiac muscle. It was found that in these striated muscles the electron opaque, final product of the histochemical reaction (PbS) was discretely deposited on the swelling of the thick elemental filaments that occurs at the M band. Additional sites of enzymatic activity occurred in mitrochondria and in round sarcoplasmic bodies. A reaction, probably non-enzymatic, also occurred in contraction bands in the area of the Z bands and in the sarcoplasmic reticulum. To ascertain the enzymatic nature of the reaction and to define the enzyme involved, control experiments were carried out and the effect of various esterase inhibitors was assayed. It is suggested that the M band enzyme is a cholinesterase, but the enzymes in the mitochondria and the sarcoplasmic bodies that hydrolyze the substrate appear to be different. A possible role of the M band enzyme is discussed.


2010 ◽  
Vol 160-162 ◽  
pp. 1358-1361
Author(s):  
Hong Zhu ◽  
Zhi Hui Qiu ◽  
Qiong Hou

An economical production process of higher N-acetylchitooligosaccharides [(GlcNAc)n, n=5~7 ] was developed with enzymatic and chemical reactions in this study. (GlcNAc)n were prepared selectively and efficiently by hydrolysis of chitosans with cheap enzyme preparations including cellulase TV, cellulosin A.C and hemicellulase, followed by N-acetylation with acetic anhydride. Higher (GlcNAc)n could be obtained in high yields by using cellulosin A.C and hemicellulase, which are originated from Aspergillus niger.


2011 ◽  
Vol 59 (5) ◽  
pp. 1924-1930 ◽  
Author(s):  
Yuezhong Wen ◽  
Chandan Li ◽  
Zhaohua Fang ◽  
Shulin Zhuang ◽  
Weiping Liu

2010 ◽  
Vol 38 (8) ◽  
pp. 975-983 ◽  
Author(s):  
Lisbeth Garbrecht Thygesen ◽  
Budi Juliman Hidayat ◽  
Katja Salomon Johansen ◽  
Claus Felby

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