Ferments and their actions / by Carl Oppenheimer ; Translated from the German by C. Ainsworth Mitchell.

Date:
1901
Catalogue details

Licence: In copyright

Credit: Ferments and their actions / by Carl Oppenheimer ; Translated from the German by C. Ainsworth Mitchell. Source: Wellcome Collection.

Provider: This material has been provided by the Royal College of Physicians of Edinburgh. The original may be consulted at the Royal College of Physicians of Edinburgh.

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    wine. It is destroyed on pasteurising the wine at 60° C., and also by sulphurous acid; this is said to partially account for the beneficial effect of sulphuring the casks (Gouirand,1 Martinand,2 Laborde,3 Cazeneuve,4 Bouffard,5 and others). Laborde identifies its activity with that of the fungus Botrytis cinerea, which, however, is disputed by Cazeneuve. Aspergillus, &c., produce no oinoxydase. Brissemoret and Jeanne6 discovered an oxydase in digitalis. Lindet7 attributes the darkening of apple-juice to an oxydase which oxidises the tannin. In considering this wholesale production of oxydases, &c., with those which the French biological chemists presented to us some years ago, we have the uneasy, dispiriting feeling that a large proportion of these enzymes would not stand the test of a close investigation, particularly since not one of them has been prepared in an approximately pure condition. The only German chemist who, to my knowledge, has studied laccase more closely is greatly inclined to attribute their “ fermentative activity ” to the long-known catalytic action of the manganese salts, of which they contain a large proportion (Ruff8). This opinion appears to be gradually gaining ground, even among the French. At least Bertrand 9 has thought the catalytic action of the manganese salts in laccase worth a fuller investigation, and ascribes great importance to them. He does not, indeed, yet abandon the specific activity of laccase, but considers that the manganese salts can only be credited with a subsidiary force, and therefore terms them co-ferments. The laccase from lucernes contains very little manganese, but also has a very weak action. He assumes that manganous oxide acts as the conveyor of oxygen, being alternately oxidised to manganese dioxide and giving up its oxygen again. The ferment itself is considered to be a salt-like compound of manganese oxide with a proteid nucleus, the former being the conveyor of the activity. He thus formulates speculations similar to those of Spitzer on his nucleo-proteids (vid'e p. 287). The theory of the oxydases also receives a severe blow by the discovery of Hasse and Framm 10 that the blue coloration of 1 Gouirand, Comptes Rendus, cxx., 887, 1895. 2 Martinand, Comptes Rendus, cxx., 1426. 3 Laborde, Comptes Rendus. cxxiii., 1074, 1896. 4 Cazeneuve, Comptes Rendus, cxxiv., 406, 781, 1897. 5 Bouffard, Comptes Rendus, cxxix., 706. 6 Brissemoret and Jeanne, Journ. Pharm. et Cliim. [6], viii., 481 ; Chem. Centralb., i., 133, 1899. 7 Lindet, Comptes Rendus, cxx., 370, 1895. 8 Ruff. Private communication. 9 Bertrand, CompAes Rendus, cxxiv., 1032, 1355, 1897. Cf. Deniges, Comptes Rendus, cxxx., 32, 1900. 10 Nasse and Framm, Pjlug. A., lxiii., 203, 1896.