Volume: 51 Issue: 1
Year: 2020, Page: 40-47,
Received: Aug. 2, 2019 Accepted: Nov. 11, 2019 Published: Jan. 1, 2020
Lactoferrin, a minor whey protein present mainly in milk as well as in small quantities in most of the secretions of the body, has a wide range of biological activities to its credit including antimicrobial, antioxidant, anticancer and immunomodulatory properties. A low molecular weight peptideisolated from the pepsin hydrolysate of lactoferrin called aslactoferricin B, has been found to be more functionally active than its parent compound. The present work focussed on the isolation of lactoferrin from the colostrumof Malabari goats by cation exchange chromatography, followed by the assessment of its molecular weight by SDS-PAGE andits characterization by dot blot assay and western blotting.The concentration of lactoferrin as estimated by Lowry’s method was found to be 15.103 mg/L of colostrum. Lactoferrin was hydrolysed by treatment with three per cent porcine pepsin under acidic conditions to form lactoferrin pepsin hydrolysate. The results of this study point to a single one step method to obtain pure lactoferrin from goats and further preparation of its pepsin hydrolysate.
Keywords: Whey proteins, lactoferrin, lactoferricin B, pepsin hydrolysate
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© 2020 Chandran et al. This is an open access article distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Chandran, D., Uma, R. and Eldho, L. 2020. Characterisation of Malabari goat lactoferrin and its pepsin hydrolysate. J. Vet. Anim. Sci. 51(1): 40-47.