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Digestion in Leidynema appendiculata (Leidy, 1850), a nematode parasitic in cockroaches

Published online by Cambridge University Press:  06 April 2009

D. L. Lee
D. L. Lee
Affiliation:
The Molteno Institute, University of Cambridge
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Extract

1. A study of the digestive enzymes present in the nematode Leidynema appendiculata, parasitic in the cockroach, gave the following results.

2. An amylase with optimum activity at pH 4·5, is present. Sodium chloride increases activity by 29 % at this pH.

3. A maltase, with maximum activity at pH 5·0–6·0, is present. It is completely inhibited by 15 % glycerin.

4. Lactase and invertase were not detected.

5. A protease, capable of clotting calcified milk, and of splitting gelatin and edestin, with maximum activity at pH 6·0, is present. KCN does not increase activity.

6. Peptidases splitting glycyl-glycine, dl-leucyl-glycine and dl-leucyl-glycyl-glycine, and a prolidase splitting glycyl-l-proline are present.

7. A lipase hydrolysing glycerol tributyrate, with maximum activity at pH 7·0 is present. Hydrolysis of olive oil and ethyl butyrate was not detected.

8. It is concluded that these enzymes are quite distinct from those of the host and that digestion probably takes place over the range of pH 5·5–6·0.

Type
Research Article
Information
Parasitology , Volume 48 , Issue 3-4 , November 1958 , pp. 437 - 447
Copyright
Copyright © Cambridge University Press 1958

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