Extracellular complex of chitinolytic enzymes of Clostridium paraputrificum strain J4 separated by membrane ultrafiltration

0347007 - ÚMCH 2011 RIV CZ eng J - Článek v odborném periodiku
Tishchenko, Galina - Koppová, Ingrid - Šimůnek, Jiří - Dohnálek, Jan
Extracellular complex of chitinolytic enzymes of Clostridium paraputrificum strain J4 separated by membrane ultrafiltration.
Folia Microbiologica. Roč. 55, č. 4 (2010), s. 386-389. ISSN 0015-5632. E-ISSN 1874-9356
Grant CEP: GA ČR(CZ) GA525/08/0803; GA ČR GA310/09/1407
Výzkumný záměr: CEZ:AV0Z40500505; CEZ:AV0Z50450515
Klíčová slova: chitinolytic enzymes * Clostridium paraputrificum * membrane diafiltration
Kód oboru RIV: FB - Endokrinologie, diabetologie, metabolizmus, výživa
Impakt faktor: 0.977, rok: 2010

Membrane diafiltration was used for separation of the extracellular complex of chitinolytic enzymes of C. paraputrificum J4 free from contaminants with molar mass higher than 100 kDa and lower than 30 kDa. The enzyme complex containing β-N-acetylglucosaminidase (NAGase) and six endochitinases was concentrated on a membrane with cut-off 30 kDa. In this retentate, the NAGase/endochitinase specific activity was 13.5/6.5-times higher than in the initial culture filtrate. NAGase (38 kDa) was less active and stable at pH lower than 4 and higher than 8 but it was more temperature-stable than endochitinases, especially at 40-60 °C. In contrast to endochitinases, the pH optimum of NAGase activity was shifted by ca. 0.7 pH units to the alkaline region. The knowledge of composition of chitinolytic enzymes, their pH and temperature stability is useful for optimization of the separation process.
Trvalý link: http://hdl.handle.net/11104/0187884