Digestion in Plants.

Otago Witness, Issue 2556, 11 March 1903, Page 64

Digestion in Plants.

This was the text of a very interesting paper read by Professor S. H. Vines at the last meeting of the Linnean Society of London. It has long been known that certain plants like the foreign Nepenthes and Sarracenip and the native sundew and butterwort possess the power to digest or absorb nitrogen from bodies of insects which they entrap by various devices, but recent researches made by Professor Vines go to show that many other plants besides these insectivorous specimens possess enzymes or ferments that enable them to digest proteid 0. albuminoid matter. In the early part of his investigations Professor Vines/ found that the enzyme in the Nepenthes not only possessed the property of peptonising the highei proteids (such as fibrin) but that it was also proteolytic, in othei words that it was capable of digesting proteids by " decomposing " o splitting up tho proteid matter into certain non-nitro-genous substances. It has now been found that quite a number of plants possess this power, among them the iurnip, the potato, the tomato, lettuce, the pear, the grape, the melon, tho cucumber, the onion, the pea, etc., etc. Having established the presence of thL proteolytic enzyme, the next step was to ascertain whether the tissues or juices of the plants under investigation were capable of peptonieinj; the highei proteids. Evidence of the ability to do so wat, obtained in the case of the juke of th. .melon, of the watery extract of the lettuce, and of the tissue of the mushroom. The results in other ,-ases were eithei doubtful or negative. There was, frequently, evidence that the proteids naturally existing in thi vegetable substances themselves had been digested. The experiments definitely establish Jie fact that an enzyme wk:ch actively proteolyses the simpler forms of proteid is present in all parts of the plant body. But the question as to the precise nature of this enzyme still remains to be answered. Where proteolysea is accomplished by peptonisation. it may be infered that the enzyme is allied to the trypsin of the animal body. Where no peptonisation, but only proteolysis, can be detected, it seems probabh tfiat the enzyme is allied to the erepsin recently discovered by Colnheim in the small intestine. Possibly more than one enzyme may be active in certain cases.

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