Počet záznamů: 1
Identification and Characterization of Clostridium paraputrificum, a Chitinolytic Bacterium of Human Digestive Tract
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SYSNO ASEP 0213466 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Ostatní články Název Identification and Characterization of Clostridium paraputrificum, a Chitinolytic Bacterium of Human Digestive Tract Tvůrce(i) Šimůnek, Jiří (UZFG-Y) RID
Kopečný, Jan (UZFG-Y) RID, ORCID
Hodrová, Blanka (UZFG-Y)
Bartoňová, Hana (UZFG-Y)Zdroj.dok. Folia Microbiologica. - : Springer - ISSN 0015-5632
Roč. 47, č. 5 (2002), s. 559-564Poč.str. 5 s. Jazyk dok. eng - angličtina Země vyd. CZ - Česká republika Klíč. slova Clostridium paraputrificum ; Chitinolytic bacterium ; digestive tract Vědní obor RIV EE - Mikrobiologie, virologie CEP KSK5020115 GA AV ČR - Akademie věd GA525/00/0984 GA ČR - Grantová agentura ČR KSK5052113 GA AV ČR - Akademie věd Anotace A strictly anaerobic, mesophilic and chitinolytic bacterial strain was isolated from human feces. Based on morphological and physiological properties and 16S rRNA sequence analysis the strain was identified as Clostridium paraputrificum.The strain utilized chitin and N-acetyl-D-glucosamine, grew on glucose and hydrolyzed starch. Cultivation of the strain with colloidal chitin as the growth substrate resulted in the production of gas and formation of acetate and lactate and only small quantities of propionate and butyrate. In the course of a 10-d cultivation with chitin, the endochitinase activity was detected after 1 d and gradually increased, reaching maximum after 3 d. The beta-N-acetylglucosaminidase activity appeared just at the beginning of the cultivation, increased to day 2 and then remained nearly constant. More than 90 of chitin added was degraded within 2 d of cultivation. On the zymogram of the extracelular chitinolytic complex were visible at least 6 isoenzymes with molar mass 43.5-65.0 kDa. The temperature optimim of endochitinase and beta-N-acetylglucosaminidase activities was 50oC - the optimum activity of both enzymes was found at pH 4-6. Pracoviště Ústav živočišné fyziologie a genetiky Kontakt Jana Zásmětová, knihovna@iapg.cas.cz, Tel.: 315 639 554 Rok sběru 2003
Počet záznamů: 1