ChemInform Abstract: Rapid, Effective Deprotection of tert-Butoxycarbonyl (Boc) Amino Acids and Peptides at High Temperatures Using a Thermally Stable Ionic Liquid.

ChemInform ◽  
2016 ◽  
Vol 47 (14) ◽  
Author(s):  
Sumit S. Bhawal ◽  
Rahul A. Patil ◽  
Daniel W. Armstrong
RSC Advances ◽  
2015 ◽  
Vol 5 (116) ◽  
pp. 95854-95856 ◽  
Author(s):  
Sumit S. Bhawal ◽  
Rahul A. Patil ◽  
Daniel W. Armstrong

A method for high temperature Boc deprotection of amino acids and peptides in a phosphonium ionic liquid is described.


Author(s):  
Ramana Murthy Palle ◽  
Jing-Cai Zhang ◽  
Wei-Zhen Li

Pd-based catalysts are efficient for methane combustion but impractical at high temperatures due to sintering effect. Here in, we report a thermally stable Pd/SBA-15 catalyst that was prepared by using...


2017 ◽  
Vol 136 ◽  
pp. 96-102 ◽  
Author(s):  
Zhihua Luo ◽  
Jingjing Pei ◽  
Longxiang Wang ◽  
Peizhi Yu ◽  
Zhangxin Chen

2020 ◽  
Vol 24 (2) ◽  
pp. 105
Author(s):  
Edvan Arifsaputra Suherman ◽  
Maelita Ramdani Moeis ◽  
Elvi Restiawaty

Endoglucanase is used in industries that apply high temperatures, such as bioethanol, detergent, paper, and animal feed industries. Most available endoglucanases have very low stability at high temperatures. Therefore, this study aimed to identfy a new thermostable endoglucanase that is able to maintain its actvity at high temperatures. Five isolates of thermophilic bacteria were previously isolated from the hydrothermal vent of West Kawio, Indonesia. Among them, the DSI2 isolate showed the highest endoglucanase actvity, and was identfed and named as Bacillus safensis DSI2. The EgDSI2 gene was cloned from B. safensis DSI2. EgDSI2 is 1851 bp long encoding a protein of 616 amino acids. The encoded protein, EgDSI2, has high sequence identty to other B. safensis endoglucanases and was predicted with the Compute pI/Mw tool to be 69.41 kDa. EgDSI2 was high in hydrophobic amino acids. The enzyme had higher percentage of Ala andPro, and lower percentage of Gly compared to thermolabile endoglucanases from two Bacillus species. EgDSI2 harbored a catalytc domain belonging to glycosyl hydrolase family 9 (GH9) and a type 3 cellulose‐binding domain (CBM3). Propertes of endoglucanases with GH9‐CBM3 modular organizaton include actvity over a wide pH range, high optmum temperature, and thermostablity. Therefore, EgDSI2 has potental applicatons in the industries.


Langmuir ◽  
2019 ◽  
Vol 35 (11) ◽  
pp. 4085-4093 ◽  
Author(s):  
Manvir Kaur ◽  
Gurbir Singh ◽  
Anupreet Kaur ◽  
Pushpender Kumar Sharma ◽  
Tejwant Singh Kang

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