Burkholderia multivorans SB6 lipase as a detergent ingredient: characterization and stabilization
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Date
2016
Authors
Journal Title
Journal ISSN
Volume Title
Publisher
SPRINGER HEIDELBERG
Access Rights
info:eu-repo/semantics/closedAccess
Abstract
In this study, 265 bacterial isolates were collected from kitchen wastewater samples using Rhodamine B agar medium. Of these, 115 isolates were found to respond positively to the addition of commercial detergents. Using 16S rRNA sequence analysis, the isolate demonstrating the high stability towards commercial detergents was identified as Burkholderia multivorans. An SB6 lipase with a molecular mass of 70 kDa was purified from B. multivorans. The purified enzyme showed optimal activity at pH 9.0 and 40 A degrees C and remained stable in the presence of various metal ions, surfactants, and oxidizing agents. The addition of boron compounds improved the pH stability and thermostability of the enzyme, which displayed stability against some commercial detergents; moreover, this stability increased when boron compounds were added to the incubation medium as stabilizers. These properties make SB6 lipase an ideal choice as an additive in detergent formulations.
Description
Keywords
Lipase, Detergent, Boron, Characterization, Stabilization
Journal or Series
JOURNAL OF SURFACTANTS AND DETERGENTS
WoS Q Value
N/A
Scopus Q Value
Q2
Volume
19
Issue
1
