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Open AccessArticle

Preparation of Stable Cross-Linked Enzyme Aggregates (CLEAs) of a Ureibacillus thermosphaericus Esterase for Application in Malathion Removal from Wastewater

1
Boreskov Institute of Catalysis (BIC), Lavrentieva ave. 5, 630090 Novosibirsk, Russia
2
Novosibirsk State University (NSU), Pirogova str. 2, 630090 Novosibirsk, Russia
*
Author to whom correspondence should be addressed.
Catalysts 2018, 8(4), 154; https://doi.org/10.3390/catal8040154
Received: 26 March 2018 / Revised: 8 April 2018 / Accepted: 8 April 2018 / Published: 11 April 2018
(This article belongs to the Special Issue Immobilized Biocatalysts)
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Abstract

In this study, the active and stable cross-linked enzyme aggregates (CLEAs) of the thermostable esterase estUT1 of the bacterium Ureibacillus thermosphaericus were prepared for application in malathion removal from municipal wastewater. Co-expression of esterase with an E. coli chaperone team (KJE, ClpB, and ELS) increased the activity of the soluble enzyme fraction up to 200.7 ± 15.5 U mg−1. Response surface methodology (RSM) was used to optimize the preparation of the CLEA-estUT1 biocatalyst to maximize its activity and minimize enzyme loss. CLEA-estUT1 with the highest activity of 29.4 ± 0.5 U mg−1 (90.6 ± 2.7% of the recovered activity) was prepared with 65.1% (w/v) ammonium sulfate, 120.6 mM glutaraldehyde, and 0.2 mM bovine serum albumin at 5.1 h of cross-linking. The biocatalyst has maximal activity at 80 °С and pH 8.0. Analysis of the properties of CLEA-estUT1 and free enzyme at 50–80 °C and pH 5.0–10.0 showed higher stability of the biocatalyst. CLEA-estUT1 showed marked tolerance against a number of chemicals and high operational stability and activity in the reaction of malathion hydrolysis in wastewater (up to 99.5 ± 1.4%). After 25 cycles of malathion hydrolysis at 37 °С, it retained 55.2 ± 1.1% of the initial activity. The high stability and reusability of CLEA-estUT1 make it applicable for the degradation of insecticides. View Full-Text
Keywords: molecular chaperones; esterase; Ureibacillus thermosphaericus; cross-linked enzyme aggregates; response surface methodology; malathion hydrolysis molecular chaperones; esterase; Ureibacillus thermosphaericus; cross-linked enzyme aggregates; response surface methodology; malathion hydrolysis
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Samoylova, Y.V.; Sorokina, K.N.; Piligaev, A.V.; Parmon, V.N. Preparation of Stable Cross-Linked Enzyme Aggregates (CLEAs) of a Ureibacillus thermosphaericus Esterase for Application in Malathion Removal from Wastewater. Catalysts 2018, 8, 154.

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