Isolation and properties of major components of Penicillium canescens extracellular enzyme complex

• Published in: Biochemistry (Moscow) Vol. 68; no. 11; pp. 1200 - 1209
• Main Authors: Sinitsyna, O A, Bukhtoyarov, F E, Gusakov, A V, Okunev, O N, Bekkarevitch, A O, Vinetsky, Yu P, Sinitsyn, A P
• Format: Journal Article
• Language: English
• Published: United States Springer Nature B.V 01-11-2003
• Subjects: beta-Galactosidase - chemistry; beta-Galactosidase - isolation & purification; Chromatography, Liquid; Electrophoresis, Polyacrylamide Gel; Endo-1,3-beta-Glucanase - chemistry; Endo-1,3-beta-Glucanase - isolation & purification; Enzymes; Fungal Proteins - chemistry; Fungal Proteins - isolation & purification; Glycoside Hydrolases - chemistry; Glycoside Hydrolases - isolation & purification; Penicillium - enzymology; Substrate Specificity
• ISSN: 0006-2979; 1608-3040
• DOI: 10.1023/b:biry.0000009134.48246.7e

The composition of the enzyme complex secreted by Penicillium canescens was investigated. A scheme for purification of the main components of the complex by chromatofocusing on a Mono P column was developed. It was found that along with beta-galactosidase, the major components of the complex were endo-beta-1,4-xylanase (31 kD, pI 8.2-9.3), alpha-L-arabinofuranosidase (60 kD, pI 7.6), arabinoxylan-arabinofuranohydrolase (70 kD, pI 3.8-4.0), and endo-beta-1,3/1,4-glucanase (40 kD, pI 4.4). The substrate specificity, pH and temperature activity optima, adsorbability, thermal stability, and ability for synergic interaction of the isolated enzymes were studied.