Purification and characterization of acid-stable protopectinase produced by Aspergillus awamori in solid-state fermentation

Citation
M. Nagai et al., Purification and characterization of acid-stable protopectinase produced by Aspergillus awamori in solid-state fermentation, BIOS BIOT B, 64(7), 2000, pp. 1337-1344
Citations number
28
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Agricultural Chemistry","Biochemistry & Biophysics
Journal title
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
ISSN journal
0916-8451 → ACNP
Volume
64
Issue
7
Year of publication
2000
Pages
1337 - 1344
Database
ISI
SICI code
0916-8451(200007)64:7<1337:PACOAP>2.0.ZU;2-F
Abstract
Aspergillus awamori IFO 4033 produced an acid-stable protopectinase in soli d-state fermentation using wheat bran as the medium. The enzyme was purifie d to a homogeneous preparation with anion-exchange, hydrophobic, and size-e xclusion chromatography, The enzyme was a monomeric protein of 52 kDa, by S DS-PAGE analysis, with an isoelectric point of pH 3.7. The optimum pH for e nzyme activity was 2.0, and it was most active at 50 degrees C (at pH 2.0) and was stable up to 50 degrees C (at pH 2.0). The enzyme showed pectin-rel easing activity toward protopectins from various origins, especially on lem on protopectin. An outstanding characteristic of the enzyme was its extreme stability in acidic conditions: the enzyme activity was not lost after inc ubating at pH 2.0 and 37 degrees C for 24 h.