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Transcriptomic study for screening genes involved in the oxidative bioconversions of Streptomyces avermitilis

Authors
Kim, Hyo-JeongChoi, Kwon-YoungJung, Da-HyeJung, Joon-YoungJung, EunOkYang, Yung-HunKim, Byung-GeeOh, Min-Kyu
Issue Date
11월-2013
Publisher
SPRINGER
Keywords
Streptomyces avermitilis; Transcriptomics; Daidzein; Biotransformation
Citation
BIOPROCESS AND BIOSYSTEMS ENGINEERING, v.36, no.11, pp.1621 - 1630
Indexed
SCIE
SCOPUS
Journal Title
BIOPROCESS AND BIOSYSTEMS ENGINEERING
Volume
36
Number
11
Start Page
1621
End Page
1630
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/101660
DOI
10.1007/s00449-013-0935-1
ISSN
1615-7591
Abstract
Streptomyces avermitilis is a well known organism producing avermectin antibiotics, and has been utilized as an industrial host for oxidation bioconversion processes. Recently, gene screening strategies related to bioconversions have received much focus, as attempts are made to optimize oxidation and biodegradation pathways to maximize yield and productivity. Here, we have demonstrated the oxidative metabolisms of three molecules, daidzein, p-coumaric acid and mevastatin, where S. avermitilis converted each substrate to 3',4',7-trihydroxyisoflavone, caffeic acid and hydroxyl-mevastatin to yield 9.3, 32.5 and 15.0 %, respectively. Microarray technology was exploited to investigate genome-wide analysis of gene expression changes, which were induced upon the addition of each substrate. Cytochrome P450 hydroxylases (pteC, cyp28 and olmB), diooxygenases (xylE, cdo1 and putatives) and LuxAB-like oxygenase were identified. One of them, cyp28, was indeed a gene encoding P450 hydroxylase responsible for the oxidative reaction of daidzein. Furthermore, possible electron transfer chain (fdrC -> pteE -> pteC) supporting cytochrome P450 dependent hydroxylation of daidzein has been suggested based on the interpretation of expression profiles. The result provided a potential application of transcriptomic study on uncovering enzymes involved in oxidative bioconversions of S. avermitilis.
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