Hostname: page-component-745bb68f8f-f46jp Total loading time: 0 Render date: 2025-02-11T13:53:01.219Z Has data issue: false hasContentIssue false

Biochemical characterization of buffalo (Bubalus bubalis) milk lysozyme

Published online by Cambridge University Press:  16 October 2003

Subhadra Priyadarshini
Affiliation:
Division of Animal Biochemistry, National Dairy Research Institute, Karnal-132001, Haryana, India
Vinod K Kansal
Affiliation:
Division of Animal Biochemistry, National Dairy Research Institute, Karnal-132001, Haryana, India
Rights & Permissions [Opens in a new window]

Extract

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

Lysozyme, a low-molecular weight basic protein, is an important component of the antibacterial system in milk. Lysozyme activity is higher in buffalo milk (60±3·9×10−3 units/ml) than in bovine milk (29·1±1·5×10−3 units/ml). Buffalo colostrum contains five-times more lysozyme activity than mature milk (Priyadarshini & Kansal, 2002a). Lysozyme activity in buffalo milk is not influenced by the parity of animal or stage of lactation, but it increases during extreme weather (winter and summer). Lysozyme in buffalo milk is more stable than in cow milk during storage and heat treatment. A sharp increase in milk lysozyme has been observed in buffaloes with sub-clinical mastitis (Priyadarshini & Kansal, 2002a).

Type
Brief Report
Copyright
© Proprietors of Journal of Dairy Research 2003