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Effect of lipase–lipase interactions in the activity, stability and specificity of a lipase from Alcaligenes sp.

Paper ID Volume ID Publish Year Pages File Format Full-Text
18319 42718 2006 6 PDF Available
Title
Effect of lipase–lipase interactions in the activity, stability and specificity of a lipase from Alcaligenes sp.
Abstract

It has been found that the lipase QL from Alcaligenes sp. presents a tendency to form very strong bimolecular aggregates (as shown by gel filtration experiments). The addition of detergents (e.g., Triton X-100) is an easy way to break this aggregate. Soluble enzyme in absence of Triton (that is, forming a dimer) was more stable than the enzyme in the presence of Triton. The lack of Triton effect on the stability of immobilized preparations of monomeric enzyme suggests that its main effect is the breakage of the aggregate. The enzyme was immobilized on supports activated with glutaraldehyde in the presence and absence of Triton X-100, to immobilized monomer, or dimers, respectively, and we have found that the properties of the immobilized preparations were very different (after exhaustive washing to eliminate the remaining Triton). When the enzyme was immobilized under conditions where the enzyme tended to form aggregates, stability was much higher, activity was also higher, and the specificity and enantioselectivity of the enzyme were quite different than when the enzyme was immobilized in the presence of Triton. The addition of detergent to the enzyme preparation produced in absence of Triton promoted a release of around 50% of the protein to the supernatant. This suggested that we can immobilize the dimer or the monomer depending on the immobilization conditions. Thus, the control of the lipase–lipase interaction during immobilization dramatically alters the final biocatalyst properties.

Keywords
Lipase QL from Alcaligenes sp.; Interfacial activation; Lipase–lipase interaction; Protein immobilization
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Effect of lipase–lipase interactions in the activity, stability and specificity of a lipase from Alcaligenes sp.
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 39, Issue 2, 26 June 2006, Pages 259–264
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us