By Health and Safety Executive (HSE)
Aiding the "5 Steps to danger Assessement" leaflet, this publication illustrates the way in which businesses went approximately their checks and the way and why they reached the choices they did.
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Extra info for 5 Steps to Risk Assessment (Leaflet Packs)
Peptides with antimicrobial activities Antimicrobial peptides have been derived from lactoferrin (Meisel, 1998). An antimicrobial peptide fragment was produced in vitro upon enzymatic cleavage of lactoferrin with pepsin. The resulting peptide had better bactericidal properties than the undigested lactoferrin, suggesting that its smaller size may facilitate access to target sites on the microbial surface. The antimicrobial activity of lactoferrin seemed to be correlated with the net positive charge on the peptide.
The physiological function of protein cross-linking is to enhance the strength of the molecular structure of proteins and protein networks. The substrate specificity of cross-linking enzymes is a key aspect in developing protein – protein cross-linking structures. Enzymes like transglutaminase and protein disulfide isomerase have a defined reaction mechanism and are therefore specific, whereas enzymes like peroxidase and lipoxygenase have a more random reaction mechanism resulting in a broad substrate specificity.
1987). , 1992). Since the S. aureus V8 protease is highly specific for glutamate residues, and as these residues are uniformly distributed in the sequence of caseins, a poor EA was not expected at these DH values. This could be due to some properties of the obtained peptides, which had the glutamyl residue at the C-terminal end. 9%) improved its EA, showing the importance of the specificity of the enzyme used. However, ES of such hydrolysates was lower than that of unmodified casein. This could be attributed to the fact that the obtained peptides were not MILK PROTEIN TAILORING 39 amphiphilic enough to impart a high stability to the emulsion.