Hostname: page-component-78c5997874-xbtfd Total loading time: 0 Render date: 2024-11-11T11:12:18.870Z 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

Extract

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

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)