Purification and partial characterisation of X-prolyl dipeptidyl aminopeptidase of Lactobacillus helveticus ITG LH1 |
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| Affiliation: | 1. Key Laboratory of Marine Biogenetic Resources, Third Institute of Oceanography, State Oceanic Administration, 178 Daxue Road, Xiamen 361005, PR China;2. Collaborative Innovation Center for Development and Utilization of Marine Biological Resources, 178 Daxue Road, Xiamen 361005, PR China;3. State Key Lab of Marine Environmental Science & Key Lab of MOE for Coast and Wetland Ecosystems, School of Life Sciences, Xiamen University, Xiamen 361005, PR China;1. Department of Pharmacy, Birla Institute of Technology & Science—Pilani, Hyderabad Campus, Jawahar Nagar, Shameerpet, Hyderabad 500078, Telangana State, India;2. Regional Agricultural Research Station, Professor Jayashankar Telangana State Agricultural University, Palem 509 215, Mahaboobnagar District, Telangana State, India;3. Department of Chemistry and Materials Science, Tokyo Institute of Technology, O-okayama, Meguro, Tokyo 152-8551, Japan;1. Department of Bioengineering, Nagaoka University of Technology, Nagaoka, Niigata 940 2188, Japan;2. Enzyme Technology Laboratory, School of Biosciences, University of Calicut, Kerala 673635, India;1. Key Laboratory of Marine Biogenetic Resources, Third Institute of Oceanography, State Oceanic Administration, 178 Daxue Road, Xiamen 361005, PR China;2. Fujian Collaborative Innovation Center for Exploitation and Utilization of Marine Biological Resources, 178 Daxue Road, Xiamen 361005, PR China;3. College of Food Science, Fujian Agriculture and Forestry University, Fuzhou 350002, PR China;4. State Key Lab of Marine Environmental Science & Key Lab of MOE for Coast and Wetland Ecosystems, School of Life Sciences, Xiamen University, Xiamen 361005, PR China |
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| Abstract: | A X-prolyl dipeptidyl aminopeptidase (EC 3.4.14.5, XPDAP) from Lactobacillus helveticus ITG LH1, a strain used for Swiss-type cheese, was purified by ion exchange and affinity chromatographies. The enzyme appeared to be a 140 kDa monomer. Optimal activity occurred at pH 7 and 40°C, but it was rapidly inactivated above 50°C. The enzyme was activated by NaCl and KCl up to 50–200 mm but its activity levelled off at higher salt concentrations. Its complete inhibition was caused by 0.1 mm HgCl2, 1 mm SnCl2 and 2.5 mm CuCl2. It was inactivated by reagents specific for serine proteases, such as phenylmethylsulfonyl fluoride and sulfhydryl group-blocking reagents. The enzyme hydrolysed p-nitroanilide-substituted X-Pro and X-Ala dipeptides, as well as β-casomorphin 1-4. |
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