Food-protein enzymatic hydrolysates possess both antimicrobial and immunostimulatory activities: a âcause and effectâ theory of bifunctionality
| Autor: | Olga V. Kislukhina, Gediminas A. Biziulevičius, Vilhelmina Žukaitė, Jurgita Kazlauskaitė |
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| Rok vydání: | 2006 |
| Předmět: |
Male
Microbiology (medical) Autolysis (biology) Protein Hydrolysates Immunology Serum albumin Models Biological Microbiology Hydrolysate Mice Adjuvants Immunologic Anti-Infective Agents Phagocytosis Casein medicine Animals Immunology and Allergy chemistry.chemical_classification Mice Inbred BALB C Bacteria biology Hydrolysis Fungi Proteolytic enzymes General Medicine Trypsin Gastrointestinal Tract Ovalbumin Infectious Diseases Enzyme Biochemistry chemistry Macrophages Peritoneal biology.protein Female Dietary Proteins Peptide Hydrolases medicine.drug |
| Zdroj: | FEMS Immunology & Medical Microbiology. 46:131-138 |
| ISSN: | 1574-695X 0928-8244 |
| DOI: | 10.1111/j.1574-695x.2005.00019.x |
| Popis: | The antimicrobial activity (the ability to activate the microbial autolytic system) and immunostimulatory activity (the ability to improve the phagocytic cell functioning) of 20 food-protein hydrolysates [five food proteins (casein, alpha-lactalbumin, beta-lactoglobulin, ovalbumin and serum albumin) hydrolyzed with four gastrointestinal proteinases (trypsin, alpha-chymotrypsin, pepsin and pancreatin)] were examined. All the food-protein hydrolysates acted antimicrobially in vitro towards all 24 microbial strains tested: autolysis of 20 naturally autolyzing strains was activated, with the autolysis activation index (K(A)) ranging from 1.04 to 22.0, while autolysis was induced to values of 2.81-56.7% in four naturally nonautolyzing strains. When given to mice per os, all the food-protein hydrolysates enhanced the phagocytosing capacity of peritoneal macrophages, with the enhancement index (K(I)) ranging from 1.02 to 1.41. A direct correlation between K(A) and K(I) was observed. We make the presumption that K(I) is a function of K(A). |
| Databáze: | OpenAIRE |
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