Production of Fusarium solani f. sp. pisi cutinase in Fusarium venenatum A3/5

Jacob Dam Sorensen; Evamaria I. Petersen; Marilyn Wiebe

doi:10.1007/s10529-007-9369-7

Production of Fusarium solani f. sp. pisi cutinase in Fusarium venenatum A3/5

Jacob Dam Sorensen, Evamaria I. Petersen, Marilyn Wiebe

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Abstract

Fusarium venenatum A3/5 was transformed using the Aspergillus niger expression plasmid, pIGF, in which the coding sequence for the F. solani f. sp. pisi cutinase gene had been inserted in frame, with a KEX2 cleavage site, with the truncated A. niger glucoamylase gene under control of the A. niger glucoamylase promoter. The transformant produced up to 21 U cutinase l−1 in minimal medium containing glucose or starch as the primary carbon source. Glucoamylase (165 U l−1 or 8 mg l−1) was also produced. Both the transformant and the parent strain produced cutinase in medium containing cutin.

Original language	English
Pages (from-to)	1227-1232
Journal	Biotechnology Letters
Volume	29
Issue number	8
DOIs	https://doi.org/10.1007/s10529-007-9369-7
Publication status	Published - 2007
MoE publication type	A1 Journal article-refereed

Keywords

Cutinase
Fusarium venenatum
Recombinant protein

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10.1007/s10529-007-9369-7

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title = "Production of Fusarium solani f. sp. pisi cutinase in Fusarium venenatum A3/5",

abstract = "Fusarium venenatum A3/5 was transformed using the Aspergillus niger expression plasmid, pIGF, in which the coding sequence for the F. solani f. sp. pisi cutinase gene had been inserted in frame, with a KEX2 cleavage site, with the truncated A. niger glucoamylase gene under control of the A. niger glucoamylase promoter. The transformant produced up to 21 U cutinase l−1 in minimal medium containing glucose or starch as the primary carbon source. Glucoamylase (165 U l−1 or 8 mg l−1) was also produced. Both the transformant and the parent strain produced cutinase in medium containing cutin.",

keywords = "Cutinase, Fusarium venenatum, Recombinant protein",

author = "Sorensen, {Jacob Dam} and Petersen, {Evamaria I.} and Marilyn Wiebe",

year = "2007",

doi = "10.1007/s10529-007-9369-7",

language = "English",

volume = "29",

pages = "1227--1232",

journal = "Biotechnology Letters",

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TY - JOUR

T1 - Production of Fusarium solani f. sp. pisi cutinase in Fusarium venenatum A3/5

AU - Sorensen, Jacob Dam

AU - Petersen, Evamaria I.

AU - Wiebe, Marilyn

PY - 2007

Y1 - 2007

N2 - Fusarium venenatum A3/5 was transformed using the Aspergillus niger expression plasmid, pIGF, in which the coding sequence for the F. solani f. sp. pisi cutinase gene had been inserted in frame, with a KEX2 cleavage site, with the truncated A. niger glucoamylase gene under control of the A. niger glucoamylase promoter. The transformant produced up to 21 U cutinase l−1 in minimal medium containing glucose or starch as the primary carbon source. Glucoamylase (165 U l−1 or 8 mg l−1) was also produced. Both the transformant and the parent strain produced cutinase in medium containing cutin.

AB - Fusarium venenatum A3/5 was transformed using the Aspergillus niger expression plasmid, pIGF, in which the coding sequence for the F. solani f. sp. pisi cutinase gene had been inserted in frame, with a KEX2 cleavage site, with the truncated A. niger glucoamylase gene under control of the A. niger glucoamylase promoter. The transformant produced up to 21 U cutinase l−1 in minimal medium containing glucose or starch as the primary carbon source. Glucoamylase (165 U l−1 or 8 mg l−1) was also produced. Both the transformant and the parent strain produced cutinase in medium containing cutin.

KW - Cutinase

KW - Fusarium venenatum

KW - Recombinant protein

U2 - 10.1007/s10529-007-9369-7

DO - 10.1007/s10529-007-9369-7

M3 - Article

SN - 0141-5492

VL - 29

SP - 1227

EP - 1232

JO - Biotechnology Letters

JF - Biotechnology Letters

IS - 8

ER -

Production of Fusarium solani f. sp. pisi cutinase in Fusarium venenatum A3/5

Abstract

Keywords

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