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PubMed1965

HAEM SYNTHASE AND COBALT PORPHYRIN SYNTHASE IN VARIOUS MICRO-ORGANISMS.

1. The preparation of a crude extract of Clostridium tetanomorphum containing cobalt porphyrin synthase but little haem-synthase activity is described. 2. The properties of cobalt porphyrin synthase in the clostridial extracts is compared with the properties of a haem synthase present in crude extracts of the yeast Torulopsis utilis. 3. Cobalt porphyrin synthase in extracts of C. tetanomorphum inserts Co(2+) ions into the following dicarboxylic porphyrins in descending order of rate of insertion: meso-, deutero- and proto-porphyrins. Esterification renders meso- and deutero-porphyrins inactive as substrates. Neither the tetracarboxylic (coproporphyrin III) nor the octacarboxylic (uroporphyrin III) compounds are converted into cobalt porphyrins by the extract, but the non-enzymic incorporation of Co(2+) ions into these two porphyrins is rapid. These extracts are unable to insert Mn(2+), Zn(2+), Mg(2+) or Cu(2+) ions into mesoporphyrin. 4. Crude extracts of T. utilis readily insert both Co(2+) and Fe(2+) ions into deutero-, meso, and proto-porphyrins. Unlike the extracts of C. tetanomorphum, these preparations catalyse the insertion of Co(2+) ions into deuteroporphyrin more rapidly than into mesoporphyrin. This parallels the formation of haems by the T. utilis extract. 5. Cobalt porphyrin synthase is present in the particulate fraction of the extracts of C. tetanomorphum but requires a heat-stable factor present in the soluble fraction. This soluble factor can be replaced by GSH. 6. Cobalt porphyrin synthase in the clostridial extract is inhibited by iodoacetamide and to a smaller extent by p-chloromercuribenzoate and N-ethylmaleimide. The haem synthases of T. utilis and Micrococcus denitrificans are also inhibited by various thiol reagents.

Biochemical Phenomena↗
PubMed1965

THE FRACTIONATION OF MYROTHECIUM VERRUCARIA CELLULASE BY GEL FILTRATION.

1. Culture filtrates from Myrothecium verrucaria have been fractionated by gel filtration on Sephadex G-75 to give three major cellulolytic components with molecular weights of about 55000, 30000 and 5300. 2. The middle component has the bulk (90%) of the total carboxymethylcellulase activity and is little affected by exposure to cotton. The other two, which are mainly responsible for the activity of the filtrate towards cotton, are removed or deactivated by exposure to it. These observations accord with the previously reported behaviour of the whole culture filtrate. There is no evidence for interconversion of, or synergism between, these components. 3. Temperature control during gel filtration is necessary for reproducible results at high resolution. The effect of a change in temperature has been explained in terms of changes in the degree of swelling of the gel particles.

Biochemical Phenomena↗
PubMed1965

HYDROLYSIS OF FIBROUS COTTON AND REPRECIPITATED CELLULOSE BY CELLULOLYTIC ENZYMES FROM SOIL MICRO-ORGANISMS.

1. The action of cell-free filtrates from Trichoderma koningii was examined on undegraded cellulose in the form of cotton fibres, on degraded cellulose in the form of cellulose powder reprecipitated from phosphoric acid and on the soluble cellulose derivative CM-cellulose. 2. The cell-free filtrates compare favourably with intact cellulolytic micro-organisms in producing complete solubilization of undegraded as well as of degraded types of cellulose. Enzymic solubilization of cotton fibres gives quantitative conversion into glucose. Cellobiase is present. 3. The early enzymic breakdown of cotton fibres is characterized by the formation of very short fibres that increase to a maximum and disappear gradually by conversion into glucose. Disintegration of cotton fibres to short fibres is assisted by shaking, and within 20hr. the enzyme converts a minor fraction (up to 16%) of substrate into soluble products and a major portion (80%) into insoluble short fibres. 4. Maximum enzymic activity on cotton fibres occurs at about pH5.0, measured by the formation of short fibres, and at about pH3.8 on reprecipitated cellulose, measured by solubilization of the substrate. 5. Gluconolactone, glucose and cellobiose fail to produce marked inhibition of the enzymic hydrolysis of cotton fibres to short fibres or of the solubilization of reprecipitated cellulose unless present in amounts comparable with or greater than the initial weight of these two forms of cellulose. 6. The heavy-metal ions Cu(2+), Hg(2+) and Fe(3+) at 2mm concentration give 80-100% decrease in the enzymic breakdown of cotton fibres, measured by the formation of short fibres. At the same concentration Hg(2+) and Fe(3+) but not Cu(2+) also produce 70-100% inhibition of the solubilization of reprecipitated cellulose. 7. The ability to hydrolyse cotton fibres to short fibres and CM-cellulose to sugars is completely lost after heating enzyme preparations for 10min. at 71 degrees .

Cellulose↗