Enzyme activities and isozyme composition of triglyceride,diglyceride and monoglyceride lipases in Periplaneta americana,Locusta migratoria and Polia adjuncta |
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| Affiliation: | 1. Food Quality and Design Group, Wageningen University and Research, 6700AA, Wageningen, the Netherlands;2. Department of Food Science and Technology, Chinhoyi University of Technology, P Bag, 7724, Chinhoyi, Zimbabwe;1. Department of Animal Science, Stellenbosch University, Private Bag X1, Matieland, 7602, South Africa;2. Fisheries Management Branch, Department of Agriculture, Forestry and Fisheries, Roggebaai, 8012, South Africa;3. Centre for Nutrition and Food Sciences, Queensland Alliance for Agriculture and Food Innovation (QAAFI), The University of Queensland, Health and Food Sciences Precinct, 39 Kessels Rd, Coopers Plains 4108, Australia;1. KU Leuven, Department of Microbial and Molecular Systems (M2S), Lab4Food, Technology Campus Geel, Kleinhoefstraat 4, B-2440 Geel, Belgium;2. KU Leuven, Leuven Food Science and Nutrition Research Centre (LFoRCe), Leuven, Belgium;3. Department of Food Technology and Nutrition, CAES, Makerere University, P.O. Box, 7062 Kampala, Uganda;1. The Key Laboratory of Mariculture (Ocean University of China), Ministry of Education, Qingdao, 266003, PR China;2. Fisheries College, Ocean University of China, 5 Yushan Road, Qingdao, 266003, PR China;1. School of Marine Sciences, Ningbo University, Ningbo, 315832, PR China;2. Key Laboratory of Aquacultural Biotechnology Ministry of Education, Ningbo University, Ningbo, 315832, PR China;1. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724, USA |
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| Abstract: | - 1.1. Measurements of maximal enzyme activities were combined with an electrophoretic study of isozyme make-up in an examination of triglyceride, diglyceride and monoglyceride lipases from the flight muscle, fat body and gut of the cockroach, Periplaneta americana and the locust, Locusta migratoria and from the flight muscle and fat body of the moth, Polia adjuncta.
- 2.2. Tri-, di- and mono-glyceride lipases were present in all tissues of the insects with diglyceride lipase ≥ triglyceride lipase activity in all cases and monoglyceride lipase ≥ diglyceride lipase activity in locust and moth.
- 3.3. In the flight muscle, a strong correlation was found between the activities of lipases and the known use of lipid as a fuel for flight in these insects. Lipase activities were lowest in the cockroach (a carbohydrate-based flight metabolism), intermediate in the locust (both carbohydrate and lipid-fueled flight), and highest in the moth (a non-feeding, lipid-catabolizing adult) flight muscle.
- 4.4. Polyacrylamide gel electrophoresis, using substrate-impregnated gels and stained for fatty acids released by lipase action, demonstrated the presence of tissue specific isozymes of tri-, di- and mono-glyceride lipases in the three insects. In addition, some, but not all, tissues showed multiple molecular forms of one or more of the lipases.
- 5.5. Diglyceride and monoglyceride lipase activities in both flight muscle and fat body of the insects coelectrophoresed suggesting the possibility that these two lipase activities might be catalyzed by a single enzyme protein.
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