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Chitinolytic enzymes from bacterium inhabiting human gastrointestinal tract - critical parameters of protein isolation from anaerobic culture
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SYSNO ASEP 0363003 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Chitinolytic enzymes from bacterium inhabiting human gastrointestinal tract - critical parameters of protein isolation from anaerobic culture Tvůrce(i) Dušková, Jarmila (UMCH-V) RID
Tishchenko, Galina (UMCH-V) RID
Ponomareva, E. (RU)
Šimůnek, Jiří (UZFG-Y) RID
Koppová, Ingrid (UZFG-Y) RID
Skálová, Tereza (UMCH-V) RID
Štěpánková, Andrea (UMCH-V)
Hašek, Jindřich (UMCH-V) RID
Dohnálek, Jan (UMCH-V) RIDZdroj.dok. Acta Biochimica Polonica - ISSN 0001-527X
Roč. 58, č. 2 (2011), s. 261-263Poč.str. 3 s. Jazyk dok. eng - angličtina Země vyd. PL - Polsko Klíč. slova chitinolytic enzymes ; anaerobic cultivation ; protein isolation Vědní obor RIV EE - Mikrobiologie, virologie CEP GA310/09/1407 GA ČR - Grantová agentura ČR GA305/07/1073 GA ČR - Grantová agentura ČR CEZ AV0Z40500505 - UMCH-V (2005-2011) AV0Z50450515 - UZFG-Y (2005-2011) UT WOS 000292350900018 Anotace The object of this study are chitinolytic enzymes produced by bacterium Clostridium paraputrificum 14 isolated from the gastrointestinal tract of a healthy human. In particular, we focus on the development of purification protocols, determination of properties of the enzymes and their activity profiles. The process of bacteria cultivation and isolation of chitinolytic complex of enzymes was optimized. A range of various purification procedures were used such as ultrafiltration, precipitation, chromatographic separations (ion-exchange, size exclusion, chromatofocusing) in altered combinations. The optimal purification protocol comprises two or three steps. Individual samples were analyzed by SDS/PAGE electrophoresis and after renaturation their activity could be detected using zymograms. Mass spectroscopy peptide fragment analysis and MALDI analysis of the purest samples indicate presence of endochitinase B (molecular mass about 85 kDa) and of 60-kDa endo- and exochitinases. Pracoviště Ústav makromolekulární chemie Kontakt Eva Čechová, cechova@imc.cas.cz ; Tel.: 296 809 358 Rok sběru 2012 Elektronická adresa http://www.actabp.pl/pdf/2_2011/261.pdf
Počet záznamů: 1