BIOCHEMICAL AND ELECTRON-MICROSCOPIC STUDIES OF THE STREPTOMYCES-RETICULI CELLULASE (AVICELASE) IN ITS MYCELIUM-ASSOCIATED AND EXTRACELLULAR FORMS
DC Element | Wert | Sprache |
---|---|---|
dc.contributor.author | SCHLOCHTERMEIER, A | |
dc.contributor.author | NIEMEYER, F | |
dc.contributor.author | SCHREMPF, H | |
dc.date.accessioned | 2021-12-23T16:02:49Z | - |
dc.date.available | 2021-12-23T16:02:49Z | - |
dc.date.issued | 1992 | |
dc.identifier.issn | 00992240 | |
dc.identifier.uri | https://osnascholar.ub.uni-osnabrueck.de/handle/unios/5627 | - |
dc.description.abstract | Streptomyces reticuli is able to grow efficiently with crystalline cellulose (Avicel) as the sole carbon source. Cultivation in the presence of the nonionic detergent Tween 80 at a concentration of 0.1% led to a 10-fold increase in extracellular cellulolytic activity. Under these conditions, one single 82-kDa cellulase (Avicelase) capable of degrading crystalline and soluble cellulose as well as cellodextrins and p-nitrophenylcellobioside was purified to apparent homogeneity by a procedure which consisted of two consecutive anion-exchange chromatographies followed by chromatofocusing. Aggregation, which was a major problem during protein purification, could be avoided by including Triton X-100 at a concentration of 0.1% in every chromatographic step. The Avicelase was identified in extracellular and mycelium-associated forms, the latter of which could be released efficiently by nonionic detergents. In addition, a 42-kDa truncated form retaining cellulolytic activity was identified which had been generated from the 82-kDa enzyme by a protease. Antibodies raised against the mycelium-associated Avicelase reacted with the 42-kDa derivative and the extracellular form. The mycelial association of the enzyme was confirmed by immunofluorescence and immunoelectron microscopies. | |
dc.language.iso | en | |
dc.publisher | AMER SOC MICROBIOLOGY | |
dc.relation.ispartof | APPLIED AND ENVIRONMENTAL MICROBIOLOGY | |
dc.subject | 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE | |
dc.subject | Biotechnology & Applied Microbiology | |
dc.subject | CELLULOLYTIC ENZYMES | |
dc.subject | CLOSTRIDIUM-THERMOCELLUM | |
dc.subject | COMPLEX | |
dc.subject | FAMILIES | |
dc.subject | GENES | |
dc.subject | Microbiology | |
dc.subject | PURIFICATION | |
dc.subject | STERCORARIUM | |
dc.subject | SYSTEM | |
dc.subject | TRICHODERMA-REESEI | |
dc.title | BIOCHEMICAL AND ELECTRON-MICROSCOPIC STUDIES OF THE STREPTOMYCES-RETICULI CELLULASE (AVICELASE) IN ITS MYCELIUM-ASSOCIATED AND EXTRACELLULAR FORMS | |
dc.type | journal article | |
dc.identifier.doi | 10.1128/AEM.58.10.3240-3248.1992 | |
dc.identifier.isi | ISI:A1992JQ65400005 | |
dc.description.volume | 58 | |
dc.description.issue | 10 | |
dc.description.startpage | 3240 | |
dc.description.endpage | 3248 | |
dc.identifier.eissn | 10985336 | |
dc.publisher.place | 1752 N ST NW, WASHINGTON, DC 20036-2904 USA | |
dcterms.isPartOf.abbreviation | Appl. Environ. Microbiol. | |
dcterms.oaStatus | Green Published, Bronze | |
crisitem.author.dept | FB 05 - Biologie/Chemie | - |
crisitem.author.deptid | fb05 | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.netid | ScHi752 | - |
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