SELDI-TOF-MS as a rapid tool to study food related protein–peptide interactions |
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| Authors: | HA Kosters PA Wierenga H Gruppen |
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| Affiliation: | 1. TI Food & Nutrition, P.O. Box 557, 6700 AN Wageningen, The Netherlands;2. Laboratory of Food Chemistry, Wageningen University, P.O. Box 8129, 6700 EV Wageningen, The Netherlands;3. NIZO Food Research B.V., P.O. Box 20, 6710 BA Ede, The Netherlands;1. CSIRO Materials Science and Engineering, Commonwealth Scientific and Industrial Research Organization, Victoria, Australia;2. Department of Pathology, Melbourne University, Victoria, Australia;3. Vascular Biology Research Group, Department of Medical Biology, Faculty of Health Sciences, University of Tromsø, Tromsø, Norway;1. Institute of Food Quality and Food Safety, Research Center for Emerging Infections and Zoonoses (RIZ), University of Veterinary Medicine Hannover, Bischofsholer Damm 15, 30173 Hannover, Germany;2. Institut für Pharmakologie und Toxikologie, Justus-Liebig-Universität Gießen, Schubertstr 81, 35392 Gießen, Germany;3. SAC Consulting Veterinary Services, Drummondhill, Stratherrick Road, Inverness IV2 4JZ, UK;4. Animal Health and Veterinary Laboratories Agency, Penrith Regional Laboratory, Merrythought, Calthwaite, Penrith CA11 9RR, UK;5. Institut für Hygiene und Infektionskrankheiten der Tiere, Justus-Liebig-Universität, Frankfurterstr. 85-91, 35392 Gießen, Germany;1. State Key Laboratory of Medical Genetics & School of Life Sciences, Central South University, Changsha 410013, China;2. State Key Laboratory of Chemo/Biosensing and Chemometrics, Hunan University, Changsha 410081, China;1. Programa de Pós-Graduação em Bioquímica, Instituto de Química, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil;2. Departamento de Microbiologia Geral, Instituto de Microbiologia Paulo de Góes, Centro de Ciências da Saúde, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil;3. The Inorganic Pharmaceutical and Biomimetic Research Centre, Focas Research Institute, Dublin Institute of Technology, Dublin, Ireland;4. Laboratório Interdisciplinar de Pesquisas Médicas, Instituto Oswaldo Cruz, Fundação Oswaldo Cruz, Rio de Janeiro, Brazil;5. Departamento de Patologia e Programa de Pós-Graduação em Doenças Infecciosas, Universidade Federal do Espírito Santo, Espírito Santo, Brazil;6. Departamento de Microbiologia Médica, Instituto de Microbiologia Paulo de Góes, Centro de Ciências da Saúde, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil;1. Key Laboratory of Industrial Biotechnology, Ministry of Education, Jiangnan University, Wuxi 214122, China;2. Lab of Brewing Science and Technology, School of Biotechnology, Jiangnan University, Wuxi 214122, China;1. Department of Clinical Pharmacokinetics, Hoshi University, Japan;2. Division of Applied Pharmaceutical Education and Research, Hoshi University, Japan |
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| Abstract: | The use of SELDI-TOF-MS was investigated as a rapid tool to detect peptides present in a crude protein hydrolysate, which are capable to bind to intact food proteins. A purified and well characterized β-lactoglobulin preparation was extensively hydrolyzed by the Glu-specific enzyme V8 from Staphylococcus aureus. Characterization of this hydrolysate by SELDI-TOF-MS and MALDI-TOF-MS resulted in sixteen identified peptides, which covered 98% of the primary sequence of β-lactoglobulin. To identify peptides capable to bind non-covalently to intact proteins, the complete hydrolysate was applied to covalently bound ovalbumin, glycinin, β-lactoglobulin and β-casein on a SELDI ProteinChip PS-20. Six peptides (AB f29–45], AB f90–108], AB f138–158], B f63–89], AB f1–45], AB f135–162] bound to these four different proteins with decreasing affinity to glycinin > ovalbumin > β-lactoglobulin > β-casein. Peptides, which bound to these proteins were AB f1–45] and AB f135–158]. Using different concentrations of Triton X-100 (up to 2%) as a washing step prior to MS detection, enabled a rapid distinction between the peptides bound with respect to protein binding capacity. |
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