Characterization of Acyl-CoA oxidases from the lipolytic yeast Candida aaseri SH14

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Title
Characterization of Acyl-CoA oxidases from the lipolytic yeast Candida aaseri SH14
Author(s)
Z H Ibrahim; Jung Hoon BaeBong Hyun SungMi-Jin Kim; A H A Rashid; Jung Hoon Sohn
Bibliographic Citation
Journal of Microbiology and Biotechnology, vol. 32, no. 7, pp. 949-954
Publication Year
2022
Abstract
The lipolytic yeast Candida aaseri SH14 contains three Acyl-CoA oxidases (ACOXs) which are encoded by the CaAOX2, CaAOX4, and CaAOX5 genes and catalyze the first reaction in the β-oxidation of fatty acids. Here, the respective functions of the three CaAOX isozymes were studied by growth analysis of mutant strains constructed by a combination of three CaAOX mutations in minimal medium containing fatty acid as the sole carbon source. Substrate specificity of the CaAOX isozymes was analyzed using recombinant C. aaseri SH14 strains overexpressing the respective genes. CaAOX2 isozyme showed substrate specificity toward short- and medium-chain fatty acids (C6-C12), while CaAOX5 isozyme preferred long-chain fatty acid longer than C12. CaAOX4 isozyme revealed a preference for a broad substrate spectrum from C6-C16. Although the substrate specificity of CaAOX2 and CaAOX5 covers medium- and long-chain fatty acids, these two isozymes were insufficient for complete β-oxidation of long-chain fatty acids, and therefore CaAOX4 was indispensable.
Keyword
Acyl-CoA oxidaseLipolytic yeastCandida aaseriβ-oxidationSubstrate specificity
ISSN
1017-7825
Publisher
Korea Soc-Assoc-Inst
DOI
http://dx.doi.org/10.4014/jmb.2205.05029
Type
Article
Appears in Collections:
Synthetic Biology and Bioengineering Research Institute > Synthetic Biology Research Center > 1. Journal Articles
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