Production of cutinase by Thermomonospora fusca ATCC 27730

Ten strains belonging to various Thermomonospora species were tested for their ability to hydrolyse the insoluble plant polyester cutin. One strain, the thermophile T. fusca ATCC 27730, was found to produce a highly inducible cutinase when grown in broth medium containing purified apple cv. Golden D...

Full description

Saved in:
Bibliographic Details
Published in:Journal of applied microbiology 1999-04, Vol.86 (4), p.561-568
Main Authors: Fett, W.F, Wijey, C, Moreau, R.A, Osman, S.F
Format: Article
Language:English
Subjects:
apples
bacterial proteins
Biological and medical sciences
Biology of microorganisms of confirmed or potential industrial interest
Biotechnology
cutin
cutinase
enzymatic hydrolysis
enzyme activity
Fundamental and applied biological sciences. Psychology
Miscellaneous
Mission oriented research
polyesters
suberin
Thermobifida fusca
Thermomonospora fusca
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Ten strains belonging to various Thermomonospora species were tested for their ability to hydrolyse the insoluble plant polyester cutin. One strain, the thermophile T. fusca ATCC 27730, was found to produce a highly inducible cutinase when grown in broth medium containing purified apple cv. Golden Delicious cutin. Apple pomace, tomato peel, potato suberin and commercial cork were also shown to induce cutinase production. Addition of glucose to the culture medium either at the beginning of fermentation or after 2 days of incubation in the presence of apple cutin led to repression of cutinase production. The cutinase was active against a wide range of cutins, including those isolated from other apple cultivars as well as tomato, cucumber, grapefruit, and green pepper. Cutinase activity in the induced culture supernatant fluids exhibited a half-life of over 60 min at 70 degrees C and a pH optimum of 11.0.Some potential applications for cutinases are discussed.
ISSN:1364-5072
1365-2672
DOI:10.1046/j.1365-2672.1999.00690.x