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Catalysts 2017, 7(3), 91; doi:10.3390/catal7030091

Stabilization of a Lipolytic Enzyme for Commercial Application

1
Henry Wellcome Building for Biocatalysis, Biosciences, College of Life and Environmental Sciences, University of Exeter, Stocker Road, Exeter EX4 4QD, UK
2
Unilever R&D, HomeCare Discover, Disruptive Biotechnology, Quarry Road East, Bebington CH63 3JW, UK
*
Author to whom correspondence should be addressed.
Academic Editor: David D. Boehr
Received: 26 January 2017 / Revised: 6 March 2017 / Accepted: 10 March 2017 / Published: 21 March 2017
(This article belongs to the Special Issue Immobilized Enzymes: Strategies for Enzyme Stabilization)
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Abstract

Thermomyces lanouginosa lipase has been used to develop improved methods for carrier-free immobilization, the Cross-Linked Enzyme Aggregates (CLEAs), for its application in detergent products. An activator step has been introduced to the CLEAs preparation process with the addition of Tween 80 as activator molecule, in order to obtain a higher number of the individual lipase molecules in the ”open lid” conformation prior to the cross-linking step. A terminator step has been introduced to quench the cross-linking reaction at an optimal time by treatment with an amine buffer in order to obtain smaller and more homogenous cross-linked particles. This improved immobilization method has been compared to a commercially available enzyme and has been shown to be made up of smaller and more homogenous particles with an average diameter of 1.85 ± 0.28 µm which are 129.7% more active than the free enzyme. The CLEAs produced show improved features for commercial applications such as an improved wash performance comparable with the free enzyme, improved stability to proteolysis and a higher activity after long-term storage. View Full-Text
Keywords: enzyme stabilization; CLEAs; lipase; industrial application enzyme stabilization; CLEAs; lipase; industrial application
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MDPI and ACS Style

De Rose, S.A.; Novak, H.; Dowd, A.; Singh, S.; Lang, D.A.; Littlechild, J. Stabilization of a Lipolytic Enzyme for Commercial Application. Catalysts 2017, 7, 91.

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