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1.
J Sci Food Agric ; 96(3): 868-77, 2016 Feb.
Article in English | MEDLINE | ID: mdl-25754585

ABSTRACT

BACKGROUND: The aim of the present study was to generate and identify potential anti-inflammatory peptides from bovine ß-casein with enzyme preparations from cod and hog. Furthermore, the potential of cod trypsin, derived from fishery by-products, to produce these bioactive peptides for replacement of non-food-grade tosyl phenylalanyl chloromethyl ketone (TPCK)-treated porcine trypsin enzyme preparation was evaluated. RESULTS: Potential anti-inflammatory peptides were obtained by hydrolysis of ß-casein with the tryptic enzyme preparations cod trypsin, porcine trypsin (TPCK-treated) and a porcine trypsin and chymotrypsin preparation (PTN 6.0 S). Proteolysates generated with enzyme preparations containing mainly chymotryptic activity (Cryotin, Cryotin F) did not exhibit any effect. CONCLUSION: The more chymotryptic enzyme activity is present, the lower is the potential anti-inflammatory activity of the hydrolysates in HEK(nfκb-RE) cells. Comparable peptides were produced by application of porcine trypsin (TPCK) and cod trypsin. Therefore, the enzyme preparation cod trypsin can replace the non-food-grade porcine enzyme preparation trypsin (TPCK) for the generation of potential anti-inflammatory peptides from ß-casein.


Subject(s)
Anti-Inflammatory Agents/metabolism , Caseins/metabolism , Gadus morhua , Peptides/metabolism , Serine Endopeptidases/metabolism , Swine , Amino Acid Sequence , Animals , Anti-Inflammatory Agents/pharmacology , Cattle , Cell Line , Chymotrypsin/metabolism , Food-Processing Industry , Humans , Hydrolysis , Industrial Waste , Molecular Sequence Data , Peptide Fragments/chemistry , Peptide Fragments/pharmacology , Peptides/chemistry , Peptides/pharmacology , Trypsin/metabolism
2.
J Agric Food Chem ; 56(2): 461-8, 2008 Jan 23.
Article in English | MEDLINE | ID: mdl-18163564

ABSTRACT

Surface hydrophobicity (SH) of milk proteins treated physicochemically (by heating and Maillard reaction) or modified enzymatically (by transglutaminase, lactoperoxidase, laccase, and glucose oxidase) was assessed in relation to their techno-functional properties. Heat-treatment increased SH of whey protein isolate and decreased SH of sodium caseinate and bovine serum albumin. Maillard reaction of milk proteins caused time-depended decreases of SH. Only for total milk protein reacting with glucose and lactose elevated SH-values were detected. Protein modification with transglutaminase, laccase, and lactoperoxidase strongly increased the SH of whey protein isolate and total milk protein. Incubation with glucose oxidase elevated SH values of sodium caseinate, whey protein isolate, and total milk protein. When correlating SH with techno-functional properties, a positive correlation was observed between SH and foam formation, and a negative correlation was observed between SH and foam stability as well as emulsion stability. No clear correlation was detected between SH and emulsifying activity, surface tension, viscosity, and heat stability of enzymatically and physicochemically treated milk proteins.


Subject(s)
Food Technology , Milk Proteins/chemistry , Chemical Phenomena , Chemistry, Physical , Glucose Oxidase/metabolism , Hot Temperature , Hydrophobic and Hydrophilic Interactions , Laccase/metabolism , Lactoperoxidase/metabolism , Maillard Reaction , Milk Proteins/metabolism , Transglutaminases/metabolism
3.
Nahrung ; 47(5): 349-53, 2003 Oct.
Article in English | MEDLINE | ID: mdl-14609093

ABSTRACT

The paper describes studies on the influence of heat impact in reconstituted skim milk on chemical and functional properties of yoghurt products. Reconstituted skim milk was heated for 20 min at 85 degrees C, 90 degrees C, or 95 degrees C. Ropy (producing exopolysaccharides, EPS) or non-ropy strains of S. thermophilus and L. delbrueckii subsp. bulgaricus were used as starter culture for yoghurt manufacture. The studies have shown that the fermentation times decreased with increasing heat impact when the ropy starter culture was used, while they remained to a far extent unchanged if the non-ropy starter culture was applied. The lactic acid contents of the yoghurt products were in the same range when the milk was heated at 85 degrees C or 90 degrees C, while they were different when milk was heated at 95 degrees C. There was a tendency visible that an increase in preheating leads to increased L(+)- and decreased D(-)-lactic acid contents if the non-ropy culture was applied. Using the ropy culture, it was vice versa. A slightly decrease in proteolysis with increasing heat impact was to be noted with both starter cultures. Concerning the relation of proteolysis to acidification, the fermentation process could be subdivided into three sections with different slopes if the non-ropy starter culture was used, while a linear relation was found if the ropy starter culture was applied. Regarding final product characteristics it was found that the functional properties of yoghurt decreased with increasing heat impact when the ropy starter culture was applied, while they remained to a far extent unchanged when the non-ropy starter culture was used. It can be concluded from these studies that a preheating of milk at a temperature of 85 degrees C (20 min) is optimal in regard to final yoghurt product characteristics.


Subject(s)
Lactobacillus/metabolism , Milk Proteins/metabolism , Milk/chemistry , Streptococcus/metabolism , Yogurt/microbiology , Animals , Cultured Milk Products/chemistry , Fermentation , Food Handling/methods , Food Microbiology , Hot Temperature/adverse effects , Hydrogen-Ion Concentration , Polysaccharides, Bacterial/metabolism , Rheology , Time Factors
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