scispace - formally typeset

JournalISSN: 1001-3555

Journal of Molecular Catalysis 

About: Journal of Molecular Catalysis is an academic journal. The journal publishes majorly in the area(s): Catalysis & Rhodium. It has an ISSN identifier of 1001-3555. Over the lifetime, 3800 publication(s) have been published receiving 77665 citation(s).
Papers
More filters


Journal Article
TL;DR: Because the lipase can avoid the secondary hydrolysis of synthesized peptide, it is expected to be an effective method for obtaining a good yield of dipeptide.
Abstract: A dipeptide N-acetyl-l-phenylalanyl-l-tyrosinamide (N-Ac-Phe-Tyr-NH2), with angiotensin I converting enzyme (ACE) inhibitor activity, was synthesized via porcine pancreatic lipase catalyzed amidation of N-acetyl-phenylalanine ethyl ester with l-tyrosinamide in an aqueous phase. Response surface methodology was employed to evaluate the effects of synthesis parameters. The optimum synthesis conditions obtained an 84.45% yield of N-Ac-Phe-Tyr-NH2 with a reaction time of 3.8min, a temperature of 20.9°C, an enzyme amount of 6.5U, and a substrate molar ratio of 2.5:1 (Tyr:Phe). The kinetics of lipase and α-chymotrypsin catalyzed amidation was compared using the Ping-Pong mechanism. The lipase showed a lower apparent kinetic constant than α-chymotrypsin indicating that the acyl lipase intermediate had a higher affinity toward tyrosinamide in the amidation. In addition, because the lipase can avoid the secondary hydrolysis of synthesized peptide, it is expected to be an effective method for obtaining a good yield of dipeptide.

5 citations


Journal Article
Abstract: Glucose isomerase (GI) plays a crucial role in the food industry as it serves as a catalyst for the conversion of glucose to fructose. Immobilized GI is often used due to increased stability as well as the expensive costs associated with free GI. In this study, GI was immobilized on silica/chitosan hybrid microspheres via simple process through in situ encapsulation. Enhanced rate of reaction was observed when the conversion of glucose to fructose was completed in 10min catalyzed by immobilized GI because most GI was located on the shell of the support. Moreover, it was found that immobilized GI exhibited better pH, temperature, ions, storage and operation stability when compared to free GI. The relative enzyme activity was found to be above 90% with a wide pH range of 5.8–8.0, temperature range of 40–80°C, storage range of 3 months and an increase in operation range of >15 times. Therefore, immobilized GI supported by silica/chitosan hybrid microspheres is an ideal candidate for biocatalysis.

20 citations


Journal Article
Abstract: Biocatalytic oxidations can offer clear advantages compared to chemically catalyzed oxidations in terms of chemo, regio and stereoselectivity as well as a reduced environmental impact. One of the most industrially important reactions is the oxidation of alcohols, which can be carried out using alcohol dehydrogenases. However, their effective use requires an effective regeneration of the oxidized nicotinamide cofactor (NAD(P)⁺), which is critical for the economic feasibility of the process. NAD(P)H oxidase is an enzyme class of particular interest for this cofactor regeneration since it enables the use of molecular oxygen as a substrate, generating either water or hydrogen peroxide as a by-product. The use of these enzymes is now gaining an increased interest, and several different enzymes of both types have been applied for proof-of-concept. In this review, we give an overview of the state-of-the-art, and discuss several important issues for future implementation in a production process.

31 citations


Journal Article
TL;DR: A unique, one step protocol for room temperature immobilization of enzyme catalase onto epoxy functionalised cellulose matrix developed via gamma radiation induced simultaneous irradiation grafting of Glycidylmethacrylate (GMA).
Abstract: The work highlights a unique, one step protocol for room temperature immobilization of enzyme catalase onto epoxy functionalised cellulose matrix developed via gamma radiation induced simultaneous irradiation grafting of Glycidylmethacrylate (GMA). Effect of grafting parameters, such as radiation dose, monomer concentration and solvent composition on the grafting yield, was studied in order to optimize the radiation grafting process. Poly(GMA)-g-cellulose matrices were characterized by grafting yield determination, FTIR, SEM and TGA techniques. The epoxy functionalized poly(GMA)-g-cellulose matrix was subsequently employed for covalent immobilization of an industrially relevant enzyme catalase. The catalytic activity of catalase-immobilized-poly(GMA)-g-cellulose was assayed by spectrophotometrically monitoring the enzymatic degradation of H2O2 at 240nm. Catalase-immobilized-poly(GMA)-g-cellulose was observed to be reusable for over 5 cycles within ten days. Catalase was observed to show improved activity at higher pH after immobilization. Thermal stability of Catalase-immobilized-poly(GMA)-g-cellulose was also enhanced in comparison to the free enzyme system.

Network Information
Related Journals (5)
Journal of Catalysis

18.2K papers, 1M citations

83% related
Applied Catalysis A-general

13.6K papers, 603K citations

83% related
Journal of Organometallic Chemistry

39K papers, 756.2K citations

82% related
Catalysis Today

13.6K papers, 561.9K citations

81% related
Coordination Chemistry Reviews

5.7K papers, 553.1K citations

80% related
Performance
Metrics
No. of papers from the Journal in previous years
YearPapers
20201
20168
201523
201413
201314
201212