Abstract
The lipolytic activity in homogenates and aqueous extracts of acetone powders of eggs of the southern corn rootworm (Diabrotica undecimpunctata howardi Barber) was studied. The general properties were determined using as substrate olive oil in an emulsion stabilized by gum arabic. Bovine serum albumin or Triton X-100 were required in the assay system; they protected the enzyme from spontaneous denaturation. The lipase had activity optima at pH 7 and at 45 C. The preparation was inactive towards triacetin, and activity increased in the series tripropionin<tributyrin<trihexanoin< trioctanoin<tridecanoin. Activity towards tridecanoin. Triolein was hydrolyzed to oleic acid and glycerol with no marked accumulation, even transient, of partial glycerides.
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Krysan, J.L., Guss, P.L. Lipase from egg of southern corn rootworm. Lipids 8, 369–373 (1973). https://doi.org/10.1007/BF02531710
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DOI: https://doi.org/10.1007/BF02531710