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Novel antibacterial lactoferrin peptides generated by rennet digestion and autofocusing technique
Authors:Hend A Elbarbary  Adham M Abdou  Eun Young Park  Yasushi Nakamura  Hamdi A Mohamed  Kenji Sato
Affiliation:1. Division of Applied Life Sciences, Graduate School of Life & Environmental Sciences, Kyoto Prefectural University, Shimogamo, Kyoto 606-8522, Japan;2. Department of Food Control, Faculty of Veterinary Medicine, Benha University, Moshtohor, Kaliobiya 13736, Egypt;1. Instituto de Química, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil;2. Laboratório de Biologia Cardiovascular, Departamento de Farmacologia, Universidade Federal de Santa Catarina, Florianópolis, Brazil;3. Embrapa Agroindústria de Alimentos, Rio de Janeiro, Brazil;4. Embrapa Agroindústria Tropical, Fortaleza, Brazil;1. Université de Lorraine, LIBio, Laboratoire d’Ingénierie des Biomolécules, 2, av de la Forêt de Haye, TSA 40602, F-54518, Vand?uvre-lès-Nancy, France;2. University of Queensland, School of Agricultural and Food Science, St. Lucia, Queensland, 4072, Australia;1. INRA, UMR1253 Science et Technologie du Lait et de l’?uf, F-35042 Rennes, France;2. Agrocampus Ouest, UMR1253 Science et Technologie du Lait et de l’?uf, F-35042 Rennes, France;3. Univ. Paris Sud-CNRS Supélec, UMR8506 Laboratoire des Signaux et Systèmes, F-91192 Gif-sur-Yvette, France;4. INRA, UMR1019, CRNH Auvergne, F-63000 Clermont-Ferrand, France;5. Clermont Univ., Univ. d’Auvergne, Unité de Nutrition Humaine, BP 10448, F-63000 Clermont-Ferrand, France;6. INRA, UR314 Mathématiques et Informatique Appliquées, F-78352 Jouy en Josas, France;7. INRA, UMR782 Génie et Microbiologie des Procédés Alimentaires, F-78850 Thiverval Grignon, France;8. AgroParisTech, UMR782 Génie et Microbiologie des Procédés Alimentaires, F-78850 Thiverval Grignon, France;1. Istituto di Scienze dell’Alimentazione (ISA) – CNR, Via Roma 52 A/C, I-83100 Avellino, Italy;2. Dipartimento di Agraria, University of Naples “Federico II”, Parco Gussone, I-80055 Portici, Italy
Abstract:Bovine lactoferrin was hydrolysed with a range of proteolytic enzymes including calf rennet, fungal rennin, and porcine pepsin. Lactoferrin hydrolysates were assessed for their antibacterial activities against Escherichia coli and Bacillus subtilis. At pH 3, calf rennet lactoferrin hydrolysate before (LFH) showed the highest antimicrobial activity, then pepsin LFH, while fungal rennin LFH was the least active. The calf rennet and pepsin LFH were fractionated using autofocusing and chromatographic techniques. The activity-guided fractionation of calf rennet LFH identified a potent antimicrobial peptide of 11-residues, lactoferricin B (Lf-cin B), and three other novel antibacterial peptides. The 11-residues Lf-cin B was the most potent antibacterial peptide and was isolated from both rennet and pepsin LFH. Pepsin LFH had a main antimicrobial peptide of 25-residues, which was not detected in calf rennet LFH. It could be concluded that calf rennet LFH had stronger antibacterial properties than porcine pepsin LFH. Besides, autofocusing could be used for scaling up the isolation of the potent rennet LFH peptides that would have a widespread commercial use as a natural food preservative substituting porcine pepsin digest, especially in Islamic communities.
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