Enzymatic Hydrolysis of N-Benzoyl-l-Tyrosine p-Nitroanilide by α-Chymotrypsin in DMSO-Water/AOT/n-Heptane Reverse Micelles. A Unique Interfacial Effect on the Enzymatic Activity

Langmuir ◽  
2013 ◽  
Vol 29 (26) ◽  
pp. 8245-8254 ◽  
Author(s):  
Fernando Moyano ◽  
Evangelina Setien ◽  
Juana J. Silber ◽  
N. Mariano Correa
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.


2006 ◽  
Vol 1764 (6) ◽  
pp. 1029-1035 ◽  
Author(s):  
Nan Chen ◽  
Jun-Bao Fan ◽  
Jin Xiang ◽  
Jie Chen ◽  
Yi Liang

Author(s):  
Marcin Lukasiewicz ◽  
Anna Osowiec ◽  
Magdalena Marciniak

2018 ◽  
Author(s):  
Ángel Batallas ◽  
Erenio González ◽  
Carmen Salvador ◽  
Jonathan Villavicencio ◽  
Humberto González Gavilánez ◽  
...  

2019 ◽  
Vol 15 (3) ◽  
pp. 296-303 ◽  
Author(s):  
Swapnil Gaikwad ◽  
Avinash P. Ingle ◽  
Silvio Silverio da Silva ◽  
Mahendra Rai

Background: Enzymatic hydrolysis of cellulose is an expensive approach due to the high cost of an enzyme involved in the process. The goal of the current study was to apply magnetic nanomaterials as a support for immobilization of enzyme, which helps in the repeated use of immobilized enzyme for hydrolysis to make the process cost-effective. In addition, it will also provide stability to enzyme and increase its catalytic activity. Objective: The main aim of the present study is to immobilize cellulase enzyme on Magnetic Nanoparticles (MNPs) in order to enable the enzyme to be re-used for clean sugar production from cellulose. Methods: MNPs were synthesized using chemical precipitation methods and characterized by different techniques. Further, cellulase enzyme was immobilized on MNPs and efficacy of free and immobilized cellulase for hydrolysis of cellulose was evaluated. Results: Enzymatic hydrolysis of cellulose by immobilized enzyme showed enhanced catalytic activity after 48 hours compared to free enzyme. In first cycle of hydrolysis, immobilized enzyme hydrolyzed the cellulose and produced 19.5 ± 0.15 gm/L of glucose after 48 hours. On the contrary, free enzyme produced only 13.7 ± 0.25 gm/L of glucose in 48 hours. Immobilized enzyme maintained its stability and produced 6.15 ± 0.15 and 3.03 ± 0.25 gm/L of glucose in second and third cycle, respectively after 48 hours. Conclusion: This study will be very useful for sugar production because of enzyme binding efficiency and admirable reusability of immobilized enzyme, which leads to the significant increase in production of sugar from cellulosic materials.


2020 ◽  
Vol 204 ◽  
pp. 106407 ◽  
Author(s):  
Shengxin An ◽  
Wenzhi Li ◽  
Fengyang Xue ◽  
Xu Li ◽  
Ying Xia ◽  
...  

2013 ◽  
Vol 85 (17) ◽  
pp. 8121-8126 ◽  
Author(s):  
Britta Opitz ◽  
Andreas Prediger ◽  
Christian Lüder ◽  
Marrit Eckstein ◽  
Lutz Hilterhaus ◽  
...  

2014 ◽  
Vol 98 (12) ◽  
pp. 5765-5774 ◽  
Author(s):  
Yaping Shang ◽  
Rongxin Su ◽  
Renliang Huang ◽  
Yang Yang ◽  
Wei Qi ◽  
...  

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