Changes of lipase‐catalyzed lipolytic rates in a batch reactor

Wang, Y. J.; Wang, F. F.; Sheu, Jia‐Yuh; Tsai, Ying-Chieh; Shaw, Jei‐Fu

doi:10.1002/bit.260391108

Cited by 16 publications

(1 citation statement)

References 16 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…They have become increasingly important in biotechnology (1,2). The characteristic properties such as substrate specificity, regioselectivity, and enantioselectivity among various lipases allow wide applications such as in the production of emulsifiers (3,4), fatty acid esters (5), fatty acids (6)(7)(8), and carbohydrate derivatives (9,10). A Ser-His-Asp catalytic triad occurs in lipases, which are responsible for hydrolyzing triglycerides into diglycerides and subsequently, monoglycerides and free fatty acids (11).…”

mentioning

confidence: 99%

Site‐directed mutagenesis of a highly active Staphylococcus epidermidis lipase fragment identifies residues essential for catalysis

Chang

Chou

Shaw

2000

J Americ Oil Chem Soc

View full text Add to dashboard Cite

A fragment of Staphylococcus epidermidis lipase gene (Lys-303 to Lys-688) was inserted into plasmid pET-20b(+). The resulting C-terminal His-tagged recombinant protein (43 kDa) was overexpressed in Escherichia coli BL21(DE3) as a highly active lipase and was purified with nickel-coupled resin. Putative catalytic sites were determined by site-directed mutagenesis. Mutant enzymes (S418C and H648K) lost enzyme activities, which strongly suggests that the proposed residues of Ser-418 and His-648 are involved in catalysis. Site-directed mutagenesis showed that in comparison with wild-type enzyme, the M419A and V649I enzymes showed a 2.0-and 4.0-fold increase in the k cat /K m , respectively, but the M419l, M419Q, V649A, and V649L variants lost enzyme activities. The wildtype enzyme and the V649I mutant favored the hydrolysis of pnitrophenyl esters of butyrate, but the M419A favored decanoate. The results suggested that the amino acid residues (Met-419 and Val-649), following the catalytic triad, could affect the substrate specificity and/or catalytic efficiency.

show abstract

mentioning

confidence: 99%

Site‐directed mutagenesis of a highly active Staphylococcus epidermidis lipase fragment identifies residues essential for catalysis

Chang

Chou

Shaw

2000

J Americ Oil Chem Soc

View full text Add to dashboard Cite

show abstract

Catalytic Behaviour of Lipase Free and Immobilized in Biphasic Membrane Reactor with Different Low Water-Soluble Substrates

Giorno

Drioli

1997

J. Chem. Technol. Biotechnol.

View full text Add to dashboard Cite

The catalytic activity and reaction rate of lipase have been studied using the biocatalyst free in an organic/aqueous emulsion and immobilized in a biphasic organic/aqueous membrane reactor. The first reaction system was realized in a stirred tank reactor. The other was obtained by immobilizing the enzyme in the sponge layer of an asymmetric capillary membrane and recirculating the two phases along the two separate circuits of the membrane module. The performance of the reactors has been studied using two different low water‐soluble substrates: triglycerides present in commercial olive oil and (R,S)‐cyanomethyl‐[2‐(4‐isobutylphenyl)propionate] (CNE). The effects of substrate viscosity and flow dynamics conditions, such as organic phase flow rate, on the biphasic membrane reactor performance have been evaluated on the basis of observed reaction rate and catalytic activity of free and immobilized lipase for both substrates. It has been observed that free lipase showed higher catalytic activity with olive oil, while immobilized lipase showed higher catalytic activity with CNE which has a lower viscosity than olive oil. The increase of organic phase flow rate negatively affected the reactor performance, with a minor effect when using CNE rather than olive oil. The influence of temperature on the biocatalyst performance with the two substrates has also been investigated. The optimal temperature value of lipase was different for the two substrates: 28°C with CNE and 40°C with olive oil. © 1997 SCI.

show abstract

Mathematical analysis of solid–liquid mass transfer in a batch reactor for the enzymatic transformation of testosterone to 4AD

Patel

Mehra²

2002

Biotech & Bioengineering

View full text Add to dashboard Cite

A previous mathematical analysis of mass transfer in a two-phase (solid-liquid) batch reactor for enzymatic transformation of testosterone to 4AD (Pereira et al., 1987) is extended to incorporate the effect of convective mixing. The results of the analysis showed that for a given enzyme loading, the mass transfer resistance in the solid (a function of the bead size) and the intensity of convective mixing (as embodied in the mass transfer coefficient) are two parameters that can be varied such that the overall mass transfer rate from the solid to the liquid phase ensures optimal reactor performance.

show abstract

Changes of lipase‐catalyzed lipolytic rates in a batch reactor

Cited by 16 publications

References 16 publications

Site‐directed mutagenesis of a highly active Staphylococcus epidermidis lipase fragment identifies residues essential for catalysis

Site‐directed mutagenesis of a highly active Staphylococcus epidermidis lipase fragment identifies residues essential for catalysis

Catalytic Behaviour of Lipase Free and Immobilized in Biphasic Membrane Reactor with Different Low Water-Soluble Substrates

Mathematical analysis of solid–liquid mass transfer in a batch reactor for the enzymatic transformation of testosterone to 4AD

Contact Info

Product

Resources

About