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Title of Journal: Appl Microbiol Biotechnol

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Abbravation: Applied Microbiology and Biotechnology

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Springer-Verlag

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DOI

10.1016/0304-4211(77)90171-7

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1432-0614

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Engineering of LadA for enhanced hexadecane oxidat

Authors: Yanpeng Dong Jiang Yan Huiqian Du Miao Chen Ting Ma Lu Feng
Publish Date: 2012/04/12
Volume: 94, Issue: 4, Pages: 1019-1029
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Abstract

LadA a monooxygenase catalyzing the oxidation of nalkanes to 1alkanols is the key enzyme for the degradation of longchain alkanes C15–C36 in Geobacillus thermodenitrificans NG802 In this study random and sitedirected mutagenesis were performed to enhance the activity of the enzyme By screening 7500 clones from randommutant libraries for enhanced hexadecane hydroxylation activity three mutants were obtained A102D L320V and F146C/N376I By performing saturation sitedirected mutagenesis at the 102 320 146 and 376 sites six more mutants A102E L320A F146Q/N376I F146E/N376I F146R/N376I and F146N/N376I were generated Kinetic studies showed that the hydroxylation activity of purified LadA mutants on hexadecane was 2–34fold higher than that of the wildtype enzyme with the activity of F146N/N376I being the highest Effects of the mutations on optimum temperature pH and heat stability of LadA were also investigated A complementary study showed that Pseudomonas fluorescens KOB2Δ1 strains expressing the LadA mutants grew more rapidly with hexadecane than the strain expressing wildtype LadA confirming the enhanced activity of LadA mutants in vivo Structural changes resulting from the mutations were analyzed and the correlation between structural changes and enzyme activity was discussed The mutants generated in this study are potentially useful for the treatment of environmental oil pollution and in other bioconversion processesThis work was supported by the Chinese National Science Fund for Distinguished Young Scholars 30788001 the National Natural Science Foundation of China NSFC General Program Grant 30870070 30800025 and 81071392 and the National 863 Program 2009AA063502 and 2007AA02Z106

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