Fast Multipoint Immobilization of Lipase through Chiral L-Proline on MOF as Chiral Bioreactor

2021 ◽  
Author(s):  
Chia-Her Lin ◽  
Stephen Lirio ◽  
Yung-Han Shih ◽  
Pamela Berilyn So ◽  
Li-Hao Liu ◽  
...  
Keyword(s):  
Amino Acid ◽  
Porcine Pancreas ◽  
Chiral Catalyst ◽  
Porcine Pancreas Lipase ◽  
Facile Preparation

In this paper, we describe the facile preparation of a chiral catalyst by the combination of the amino acid, L-proline (Pro), and the enzyme, porcine pancreas lipase (PPL), immobilized on...

Metal-, and Organocatalyst-Free One-Pot Assembly of Chiral Aza-Tricyclic Molecules: Creating Six Contiguous Stereocenters from 2-D-Structures and an Amino Acid

2020 ◽  
Author(s):  
Dung Do
Keyword(s):  
Amino Acid ◽  
Chemical Space ◽  
Structural Diversity ◽  
Therapeutic Agents ◽  
Chiral Molecules ◽  
One Pot ◽  
Complex Molecules ◽  
Chiral Catalyst ◽  
Chiral Complex ◽  
Free Process

<p>Chiral molecules with their defined 3-D structures are of paramount importance for the study of chemical biology and drug discovery. Having rich structural diversity and unique stereoisomerism, chiral molecules offer a large chemical space that can be explored for the design of new therapeutic agents.<sup>1</sup> Practically, chiral architectures are usually prepared from organometallic and organocatalytic processes where a transition metal or an organocatalyst is tailor-made for desired reactions. As a result, developing a method that enables rapid assembly of chiral complex molecules under metal- and organocatalyst-free condition represents a daunting challenge. Here we developed a straightforward route to create a chiral 3-D structure from 2-D structures and an amino acid without any chiral catalyst. The center of this research is the design of a <a>special chiral spiroimidazolidinone cyclohexadienone intermediate</a>, a merger of a chiral reactive substrate with multiple nucleophillic/electrophillic sites and a transient organocatalyst. <a>This unique substrate-catalyst (“subcatalyst”) dual role of the intermediate enhances </a><a>the coordinational proximity of the chiral substrate and catalyst</a> in the key Aza-Michael/Michael cascade resulting in a substantial steric discrimination and an excellent overall diastereoselectivity. Whereas the “subcatalyst” (hidden catalyst) is not present in the reaction’s initial components, which renders a chiral catalyst-free process, it is strategically produced to promote sequential self-catalyzed reactions. The success of this methodology will pave the way for many efficient preparations of chiral complex molecules and aid for the quest to create next generation of therapeutic agents.</p>

Facile preparation of amine and amino acid adducts of [60]fullerene using chlorofullerene C60Cl6 as a precursor

2012 ◽  
Vol 48 (44) ◽  
pp. 5461 ◽  
Author(s):  
Alexey B. Kornev ◽  
Ekaterina A. Khakina ◽  
Sergey I. Troyanov ◽  
Alla A. Kushch ◽  
Alexander Peregudov ◽  
...  
Keyword(s):  
Amino Acid ◽  
Facile Preparation

Usage of immobilized porcine pancreas lipase in the hydrolysis of roselle (Hibiscus sabdariffa L.) seed oil

2017 ◽  
Author(s):  
Chau Tran Diem Ai ◽  
Vo Thi Hong Linh ◽  
Tran Thi Ngoc Yen ◽  
Nguyen Thi Nguyen ◽  
Phan Ngoc Hoa
Keyword(s):  
Seed Oil ◽  
Hibiscus Sabdariffa ◽  
Porcine Pancreas ◽  
Porcine Pancreas Lipase ◽  
Hydrolysis Of

scholarly journals Hydrolysis Activity of Virgin Coconut Oil Using Lipase from Different Sources

Scientifica ◽  
2018 ◽  
Vol 2018 ◽  
pp. 1-6 ◽  
Author(s):  
T. A. V. Nguyen ◽  
Truong D. Le ◽  
Hoa N. Phan ◽  
Lam B. Tran
Keyword(s):  
Time Course ◽  
Candida Rugosa ◽  
Coconut Oil ◽  
Virgin Coconut Oil ◽  
Porcine Pancreas ◽  
Hydrolysis Degree ◽  
Porcine Pancreas Lipase ◽  
Hydrolysis Process ◽  
Hydrolysis Of ◽  
Different Sources

Two types of lipase, Candida rugosa lipase (CRL) and porcine pancreas lipase (PPL), were used to hydrolyze virgin coconut oil (VCO). The hydrolysis process was carried out under four parameters, VCO to buffer ratio, lipase concentration, pH, and temperature, which have a significant effect on hydrolysis of lipase. CRL obtained the best hydrolysis condition at 1 : 5 of VCO to buffer ratio, 1.5% of CRL concentration, pH 7, and temperature of 40°C. Meanwhile, PPL gave different results at 1 : 4 of VCO to buffer ratio, 2% of lipase concentration, pH 7.5, and 40°C. The highest hydrolysis degree of CRL and PPL was obtained after 16 hours and 26 hours, reaching 79.64% and 27.94%, respectively. Besides, the hydrolysis process was controlled at different time course (every half an hour) at the first 4 hours of reaction to compare the initial hydrolysis degree of these two lipase types. FFAs from hydrolyzed products were isolated and determined the percentage of each fatty acid which contributes to the FFAs mixture. As a result, medium chain fatty acids (MCFAs) made up the main contribution in composition of FFAs and lauric acid (C12) was the largest segment (47.23% for CRL and 44.23% for PPL).

The amino acid sequence of the phospholipase A2 isoenzyme from porcine pancreas

1979 ◽  
Vol 580 (2) ◽  
pp. 411-415 ◽  
Author(s):  
W.C. Puijk ◽  
H.M. Verheij ◽  
P. Wietzes ◽  
G.H. de Haas
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Phospholipase A2 ◽  
Porcine Pancreas
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