Affordable Access

Publisher Website

Kinetics of tributyrin hydrolysis by lipase

Authors
Journal
Enzyme and Microbial Technology
0141-0229
Publisher
Elsevier
Publication Date
Volume
35
Identifiers
DOI: 10.1016/j.enzmictec.2004.08.002
Keywords
  • Bioreaction Kinetics
  • Lipase
  • Immobilized Resin
  • Enzyme Catalysis

Abstract

Abstract The kinetics for the tributyrin hydrolysis using lipase ( Pseudomonas fluorscenes CCRC-17015) were investigated in the liquid–liquid and liquid–solid–liquid reaction systems in a batch reactor. The lipase was covalently immobilized onto the surface of porous polymethylacrylamide (PMAA) crosslinking with N, N-methylene biacrylamide with a spacer of ethylenediamine actived by glutaraldehyde. The conditions such as tributyrin concentration, temperature, agitation, and pH value, were evaluated to achieve the optimum reaction conditions for both free lipase and immobilized lipase. The kinetic parameters in the reaction system were also obtained for two reaction systems. The turnover numbers calculated for free lipase and immobilized lipase were 29 and 5.7 s −1, respectively. The parameters of k and k m obtained using Lineweaver-Burk plot method were 26.2 mol/(mg min) and 1.35 mol/dm 3 for free lipase, 5.2 mol/(mg min) and 0.2 mol/dm 3 for immobilized lipase, respectively. The experimental results revealed good thermal stability, with greater stability at higher pH value for immobilized lipase in the liquid–solid–liquid reaction.

There are no comments yet on this publication. Be the first to share your thoughts.

Statistics

Seen <100 times
0 Comments

More articles like this

Reaction kinetics for the hydrolysis of tributyrin...

on Chemical Engineering Science Jan 01, 1994

Hydrolysis of emulsified tributyrin by porcine pan...

on Enzyme and Microbial Technolog... Jan 01, 1988

Hydrolysis of particulate tributyrin in a fluidize...

on Biotechnology and bioengineeri... October 1975

Kinetics of milk lipoprotein lipase. Studies with...

on European Journal of Biochemist... Nov 15, 1978
More articles like this..