PURIFICATION AND CHARACTERIZATION OF ACID PROTEINASE FROM NEOSARTORYA-FISCHERI VAR. SPINOSA IBT-4872

Authors
WU LC HANG YD
Citation
Lc. Wu et Yd. Hang, PURIFICATION AND CHARACTERIZATION OF ACID PROTEINASE FROM NEOSARTORYA-FISCHERI VAR. SPINOSA IBT-4872, Letters in applied microbiology, 27(2), 1998, pp. 71-75
Citations number
20
Categorie Soggetti
Microbiology,"Biothechnology & Applied Migrobiology
Journal title
Letters in applied microbiology → ACNP
ISSN journal
02668254
Volume
27
Issue
2
Year of publication
1998
Pages
71 - 75
Database
ISI
SICI code
0266-8254(1998)27:2<71:PACOAP>2.0.ZU;2-H
Abstract
An acid proteinase from Neosartorya fischeri var. spinosa IBT 4872 was purified 38-fold with a yield of 11% by ultrafiltration; ammonium sul phate fractionation, Sephadex-G200 gel filtration, DEAE-Sephadex anion exchange chromatography, and hydroxyapatite chromatography. The enzym e was mast active at pH 3.0 and 50 degrees C and had a molecular weigh t of 45 kDa, as determined by SDS-PAGE. It was stable over a pH range of 3.0 to 6.0 and exhibited thermal stability up to 50 degrees C. The Km value for haemoglobin was 0.44% (w/v). The activity was inhibited b y pepstatin, suggesting that the enzyme is an aspartic proteinase.