Accelerating cheese proteolysis by enriching Lactococcus lactis proteolytic system with lactobacilli peptidases |
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| Affiliation: | 1. UBSP, INRA, Domaine de Vilvert, 78352 Jouy en Josas, France;2. URLGA, INRA, Domaine de Vilvert, 78352 Jouy en Josas, France;3. FB Biologie Abt. Mikrobiologie, PO Box 3049, D-67653 Kaiserslautern, Germany;4. MTT Food Research Institute, FIN-31600 Jokioinen, Finland;5. Basic Veterinary Sciences, Section of Microbiology, P.O. Box57, 00014 Helsinki University, Finland;1. Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, People’s Republic of China;2. Key Laboratory of Structural Biology, Chinese Academy of Sciences, Hefei, Anhui 230026, People’s Republic of China;3. Innovation Center for Cell Signaling Network, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, People’s Republic of China;4. School of Pharmaceutical Sciences, Sun Yat-sen University, Guangzhou, Guangdong 510006, People’s Republic of China;1. Department of Food Science, Faculty of Science, University of Copenhagen, Rolighedsvej 26, 1958 Frederiksberg, Denmark;2. Chr. Hansen A/S, Bøge Allé 10-12, 2970 Hørsholm, Denmark;1. High Pressure and Synchrotron Radiation Physics Division, Bhabha Atomic Research Centre, Mumbai, India;2. School of Biochemistry, Devi Ahilya University, Indore, India;1. Department of Biotechnology, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, Osaka 565-0871, Japan;2. Research and Development Division, Kikkoman Corporation, 399 Noda, Noda, Chiba 278-0037, Japan;3. Division of Metabolomics, Research Center for Transomics Medicine, Medical Institute of Bioregulation, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan |
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| Abstract: | The knowledge available on the genetics and proteolytic system of lactic acid bacteria makes it possible to genetically engineer starters with increased proteolytic properties. Our objective was to identify the best available strains capable of accelerating or modulating casein proteolysis during cheese ripening.To attain this goal, we used Lactococcus lactis strains expressing 5 different Lactobacillus peptidases to ripen a cheese model. At the end of ripening, free amino acids were quantitatively and qualitatively analysed.We identified the mixture of prolidase, PepQ, and X-prolyl dipeptidyl peptidase, PepX, as well as the peptidase PepW as the most efficient peptidases to increase, up to 3-fold, the overall level of amino acids at the end of ripening. The levels of threonine, asparagine, glycine, methionine, valine, glutamine, isoleucine and proline in particular increased (more than 3.5 fold). Grouping the amino acids produced according to the specific aroma compounds that each may give rise to following an enzymatic or chemical conversion, revealed that expression of PepW or PepX and PepQ increased the amounts of all groups of amino acids while expression of PepQ or PepN increased more especially those of aromatic amino acids/proline and glutamic acid, respectively.The combination of increased proteolysis and conversion of amino acids into aroma compounds now needs to be tested. In addition, the role of proline and its derived compounds in the overall flavour of cheese should be investigated. |
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