Hydrolysis of short-chain phosphatidylcholines by bee venom phospholipase A2 |
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| Authors: | D Raykova B Blagoev |
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| Institution: | 1. School of Science and the Environment/Environmental Sciences, Grenfell Campus, Memorial University of Newfoundland, Corner Brook, Newfoundland and Labrador A2H 5G4, Canada;2. Department of Biology/Biotron Experimental Climate Change Research Centre, University of Western Ontario, London, Ontario, Canada;1. Information Technology Research Center, Beijing Academy of Agriculture and Forestry Sciences, Beijing 100097, China;2. Beijing Laboratory for Food Quality and Safety, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China;3. College of Information and Electrical Engineering, Shenyang Agricultural University, Shenyang 110866, China;4. National Engineering Research Center for Information Technology in Agriculture, Beijing Academy of Agricultural and Forestry Sciences, Beijing 100097, China;5. National Engineering Laboratory for Agri-product Quality Traceability, Beijing Academy of Agricultural and Forestry Sciences, Beijing 100097, China;6. Key Laboratory of Cold Chain Logistics Technology for Agro-product, Ministry of Agriculture and Rural Affairs, Beijing 100097, China;1. College of Food Science and Technology, Shanghai Ocean University, Shanghai 201306, China.;2. Shanghai Professional Technology Service Platform on Cold Chain Equipment Performance and Energy Saving Evaluation, Shanghai 201306, China;3. Marine Biomedical Science and Technology Innovation Platform of Lin-gang Special Area, Shanghai 201306, China |
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| Abstract: | In order to find out the aggregation state of the substrate, preferred by bee venom phospholipase A2 (EC 3.1.1.4), its action on short-chain phosphatidylcholines with two identical (C6-C10) fatty acids has been tested. The rate of hydrolysis as a function of acyl chain length showed a maximum at dioctanoylphosphatidylcholine. The effects of alcohols, NaCl and Triton X-100, which affect the aggregation state of phospholipids in water, were also studied. The addition of n-alcohol led to a significant inhibition of the hydrolysis of the substrates present in micellar form and activated the hydrolysis of substrates which form liposomes. The inhibitory effect increased with increasing length of the aliphatic carbon chain of the alcohol. Triton X-100 at low Triton/phospholipid molar ratios enhanced enzyme activity. These results do not agree with the accepted idea that bee venom phospholipase A2 hydrolyzes short-chain lecithins in their molecularly dispersed form and that micelles cannot act as substrates. The data indicate that short-chain lecithins in the aggregated state are hydrolyzed and that the requirements of bee venom phospholipase A2 for the aggregation state of the substrate are not strict. |
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