Identification and functional expression of a Δ9 fatty acid desaturase from the marine bacterium Pseudoalteromonas sp. MLY15

Yan Li; Xian Xu; Matthias Dietrich; Vlada B. Urlacher; Rolf D. Schmid; Pingkai Ouyang; Bingfang He

doi:10.1016/j.molcatb.2008.07.012

Identification and functional expression of a Δ9 fatty acid desaturase from the marine bacterium Pseudoalteromonas sp. MLY15

Yan Li, Xian Xu, Matthias Dietrich, Vlada B. Urlacher, Rolf D. Schmid, Pingkai Ouyang, Bingfang He

School of Pharmaceutical Sciences

Research output: Contribution to journal › Article › peer-review

21 Scopus citations

Abstract

A gene putatively encoding a Δ9 desaturase-like protein was cloned from the isolated marine bacterium Pseudoalteromonas sp. MLY15. The 1134 bp open reading frame, designated as PhFAD9, codes for a 377 amino acid peptide with a molecular weight of 43.4 kDa. The protein was supposed to be a membrane-bound desaturase and its possible topology model was predicted using the Phobius program. The PhFAD9 protein was confirmed to be functional with high Δ9 desaturase activity when expressed in Escherichia coli. The PhFAD9 E. coli transformant accumulated palmitoleic acid, which accounted for 91.7% of the cellular C16 fatty acids after 2 h of induction. The ability for bioconversion of stearic acid to oleic acid was also demonstrated by supplementing the medium with exogenous stearic acid.

Original language	English
Pages (from-to)	96-101
Number of pages	6
Journal	Journal of Molecular Catalysis - B Enzymatic
Volume	56
Issue number	2-3
DOIs	https://doi.org/10.1016/j.molcatb.2008.07.012
State	Published - Feb 2009

Keywords

Membrane topology
Pseudoalteromonas
Unsaturated fatty acid
Δ9 desaturase

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Access to Document

10.1016/j.molcatb.2008.07.012

Cite this

@article{61ed5f0f772b48c1ab2f77d5f38c8574,

title = "Identification and functional expression of a Δ9 fatty acid desaturase from the marine bacterium Pseudoalteromonas sp. MLY15",

abstract = "A gene putatively encoding a Δ9 desaturase-like protein was cloned from the isolated marine bacterium Pseudoalteromonas sp. MLY15. The 1134 bp open reading frame, designated as PhFAD9, codes for a 377 amino acid peptide with a molecular weight of 43.4 kDa. The protein was supposed to be a membrane-bound desaturase and its possible topology model was predicted using the Phobius program. The PhFAD9 protein was confirmed to be functional with high Δ9 desaturase activity when expressed in Escherichia coli. The PhFAD9 E. coli transformant accumulated palmitoleic acid, which accounted for 91.7% of the cellular C16 fatty acids after 2 h of induction. The ability for bioconversion of stearic acid to oleic acid was also demonstrated by supplementing the medium with exogenous stearic acid.",

keywords = "Membrane topology, Pseudoalteromonas, Unsaturated fatty acid, Δ9 desaturase",

author = "Yan Li and Xian Xu and Matthias Dietrich and Urlacher, {Vlada B.} and Schmid, {Rolf D.} and Pingkai Ouyang and Bingfang He",

year = "2009",

month = feb,

doi = "10.1016/j.molcatb.2008.07.012",

language = "英语",

volume = "56",

pages = "96--101",

journal = "Journal of Molecular Catalysis - B Enzymatic",

issn = "1381-1177",

publisher = "Elsevier",

number = "2-3",

}

TY - JOUR

T1 - Identification and functional expression of a Δ9 fatty acid desaturase from the marine bacterium Pseudoalteromonas sp. MLY15

AU - Li, Yan

AU - Xu, Xian

AU - Dietrich, Matthias

AU - Urlacher, Vlada B.

AU - Schmid, Rolf D.

AU - Ouyang, Pingkai

AU - He, Bingfang

PY - 2009/2

Y1 - 2009/2

N2 - A gene putatively encoding a Δ9 desaturase-like protein was cloned from the isolated marine bacterium Pseudoalteromonas sp. MLY15. The 1134 bp open reading frame, designated as PhFAD9, codes for a 377 amino acid peptide with a molecular weight of 43.4 kDa. The protein was supposed to be a membrane-bound desaturase and its possible topology model was predicted using the Phobius program. The PhFAD9 protein was confirmed to be functional with high Δ9 desaturase activity when expressed in Escherichia coli. The PhFAD9 E. coli transformant accumulated palmitoleic acid, which accounted for 91.7% of the cellular C16 fatty acids after 2 h of induction. The ability for bioconversion of stearic acid to oleic acid was also demonstrated by supplementing the medium with exogenous stearic acid.

AB - A gene putatively encoding a Δ9 desaturase-like protein was cloned from the isolated marine bacterium Pseudoalteromonas sp. MLY15. The 1134 bp open reading frame, designated as PhFAD9, codes for a 377 amino acid peptide with a molecular weight of 43.4 kDa. The protein was supposed to be a membrane-bound desaturase and its possible topology model was predicted using the Phobius program. The PhFAD9 protein was confirmed to be functional with high Δ9 desaturase activity when expressed in Escherichia coli. The PhFAD9 E. coli transformant accumulated palmitoleic acid, which accounted for 91.7% of the cellular C16 fatty acids after 2 h of induction. The ability for bioconversion of stearic acid to oleic acid was also demonstrated by supplementing the medium with exogenous stearic acid.

KW - Membrane topology

KW - Pseudoalteromonas

KW - Unsaturated fatty acid

KW - Δ9 desaturase

UR - http://www.scopus.com/inward/record.url?scp=57449087049&partnerID=8YFLogxK

U2 - 10.1016/j.molcatb.2008.07.012

DO - 10.1016/j.molcatb.2008.07.012

M3 - 文章

AN - SCOPUS:57449087049

SN - 1381-1177

VL - 56

SP - 96

EP - 101

JO - Journal of Molecular Catalysis - B Enzymatic

JF - Journal of Molecular Catalysis - B Enzymatic

IS - 2-3

ER -

Identification and functional expression of a Δ9 fatty acid desaturase from the marine bacterium Pseudoalteromonas sp. MLY15

Abstract

Keywords

UN SDGs

Access to Document

Other files and links

Fingerprint

Cite this