Isolation and Identification of Lactoferrin and Lactoperoxidase from the Colostrum of Indonesian Ettawa Crossbred Goat

Delivered by Ingenta to: Ahmad Nimatullah Al-Baarri IP: 114.124.199.205 On: Tue, 24 Oct 2017 02:24:30 Copyright: American Scientific Publishers Background:Lactoferrinisaglycoproteinofthetransferrinfamily which has multifunctional properties and useful for clinical and commercial application. It has some advantages as an immune system modulation, antibacterial activity and antioxidant in infant and adult as well as in animal. Lactoperoxidase is one of the most prominent enzymes in milk and catalyzes the inactivation of a wide range of microorganisms. Both lactoferrin and lactoperoxidase are expressed in most biological fluids, including colostrum. Chemical components of colostrum may vary along the days after parturition. The study of lactoferrin and lactoperoxidase from dairy goat is very limited. This study aimed to isolate and identify characteristics (the molecular weight and concentrations) of lactoferrin and lactoperoxidase from Indonesian native Ettawa crossbred goat colostrum. Method:Theisolationandpurification of lactoferrin and lactoperoxidase was conducted by an ion-exchange chromatography (SP-sepharose). Other compositions of colostrum, protein, fat and lactose concentration, were also determined. Results:The result showed that lactoferrin and lactoperoxidase concentrations in goat colostrum on the first day (317.3 mg/L and 204 mg/L) were higher than colostrum on the second day (190,5 mg/L and 61.9 mg/L) postpartum. The molecular weight of lactoferrin and lactoperoxidase were 75 and 72 kDa. Protein, fat and lactose concentrations of colostrum on the first day postpartum (6.5%, 5.7% and 4.9%) were higher than those on the second day (4.9%, 4.4% and 4.1%). Conclusion:Ahighamountoflactoferrinandlactoperoxidasecanbeisolatedfromthe goat colostrum on its first day of postpartum