Abstract:
:Both the periplasmic and the extracellular cellodextrinases from Bacteroides succinogenes S85 grown on Avicel microcrystalline cellulose were purified to homogeneity by column chromatography and characterized. Over 70% of the total cellobiosidase activity displayed by cells was accounted for by these enzymes. The periplasmic and extracellular cellodextrinases had identical molecular weights (50,000), as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and identical isoelectric points (4.9). In addition, the two enzymes were similar in catalytic properties, with K(m) and V(max) values of approximately 0.24 mM and 21 mumol/min per mg of protein, respectively. Examination of the two enzymes by using peptide mapping and immunoblotting techniques provided additional evidence indicating their identical nature. Immunoblotting of the extracellular culture fluid with affinity-purified antibody to the periplasmic cellodextrinase revealed one band with a molecular weight corresponding to that of the periplasmic cellodextrinase. The stability of the purified periplasmic cellodextrinase in aqueous solution was markedly enhanced by increased protein content. This enzyme showed a low affinity for crystalline cellulose.
journal_name
Appl Environ Microbioljournal_title
Applied and environmental microbiologyauthors
Huang L,Forsberg CWdoi
10.1128/AEM.54.6.1488-1493.1988keywords:
subject
Has Abstractpub_date
1988-06-01 00:00:00pages
1488-93issue
6eissn
0099-2240issn
1098-5336journal_volume
54pub_type
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journal_title:Applied and environmental microbiology
pub_type: 杂志文章
doi:10.1128/AEM.54.4.890-897.1988
更新日期:1988-04-01 00:00:00
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