1887

Abstract

SUMMARY: Carboxymethylcellulase (endo-1,4-β-glucanase; EC 3.2.1.4) was purified from the culture filtrate of AU-1 by (NH)SO precipitation, Avicel affinity chromatography, DEAE Sephadex G-75 chromatography and Sulphopropyl Sephadex C-50 chromatography. The enzyme was purified 36-fold and had an of 23000 as determined by gel filtration on a Sephadex G-75 column. The pH optimum of the purified enzyme was 5·5; the enzyme was stable at 65°C. Activity of the purified enzyme was significantly reduced by Cu, Pb, Sn, Ag, Hg and Fe, but was increased by 139·5% in the presence of Co. Inhibition studies indicated that the purified enzyme was either a metalloprotein or required certain metal ions for activation/stabilization; that iron was not a prosthetic group of the enzyme; that a tryptophanyl group was not involved in enzyme action; and that reduced thiol groups were required for enzyme activity and involved in the active site of the enzyme. The of the purified enzyme for carboxymethylcellulose was 4 mg ml, and the for carboxymethylcellulose hydrolysis was 0·42 mg -glucose min (mg protein).

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/content/journal/micro/10.1099/00221287-133-8-2155
1987-08-01
2019-10-23
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http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-133-8-2155
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