Isolation, Purification and Characterization of Lactoferrin from Goat Colostrum Whey

Abbas, Zainab H.; Doosh, Kifah S.; Yaseen, Nahi Y.

doi:10.3923/pjn.2015.517.523

Cited by 6 publications

(5 citation statements)

References 32 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The purity of the extracted lactoferrin was further affirmed by recovering bands in the region of 77-80 kDa, confirming that the extraction procedure gives pure lactoferrin. The results of the present study are similar to other studies conducted by Abbas et al (2015) where SDS-PAGE was used to confirm the purity of the protein (Abbas et al, 2015). Yafei et al (2011) also conducted a study based on a single band in the gel of SDS-PAGE in order to confirm the purity of the lactoferrin from defatted bovine colostrum (Liang et al, 2011).…”

Section: Discussionsupporting

confidence: 87%

Prospects of lactoferrin as potential natural antibiotic

Mimmi¹,

Areefin²,

Nasreen³

et al. 2022

Food Res.

View full text Add to dashboard Cite

Section: Discussionsupporting

confidence: 87%

Prospects of lactoferrin as potential natural antibiotic

Mimmi¹,

Areefin²,

Nasreen³

et al. 2022

Food Res.

View full text Add to dashboard Cite

“…Indonesian meat-producing goat namely Kacang goat has 73.14 kDa of lactoferrin molecular weight. 23 In the other countries, the molecular weight of lactoferrin from Pakistani native goat colostrum was approximately 80 kDa, 24 Meanwhile in Korean native goat, the lactoferrin molecular weight from colostrum was 82 kDa. 25 Furthermore, molecular weight of lactoferrin was 80 kDa in dairy cow, 26 79.5 kDa in camel 27 and 77 kDa in human.…”

Section: Discussionmentioning

confidence: 99%

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

et al. 2017

View full text Add to dashboard Cite

Background: Lactoferrin is a glycoprotein of the transferrin family 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: The isolation and purification 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: A high amount of lactoferrin and lactoperoxidase can be isolated from the goat colostrum on its first day of postpartum.

show abstract

“…Absence of any other proteins in these fractions facilitated the confirmative identification of lactoferrin by SDS-PAGE. The method of SDS-PAGE was reported to confirm the molecular weight and purity of caprine lactoferrin (Younghoon et al, 2009;Le Parc et al, 2014;Abbas et al, 2015) and that of bovine lactoferrin (Adam et al, 2008;Liang et al, 2011;Yafei et al, 2011;Moradian et al, 2014). However, the yield of lactoferrin isolated by the single-step cation exchange chromatography was found to be very less i.e., 10.94mg/L of colostrum when compared to fast protein liquid chromatography which could yield 2.4mg/mL (Moradian et al, 2014) as well as combined cation exchange gel filtration protocol which could isolate 250 mg/L of colostrum (Abbas et al, 2015).…”

Section: Discussionmentioning

confidence: 99%

Isolation and purification of lactoferrin from colostrum of Malabari goats

Vijayan¹,

Radhakrishnan²,

Eldho³

et al. 2017

JEBAS

View full text Add to dashboard Cite

Lactoferrin, an iron-binding glycoprotein, primarily present in milk, has been shown to be involved in various physiological and protective function including roles in iron homeostasis, cell proliferation, antibacterial, antifungal, antiviral, antioxidant, immunomodulatory and anticancer activities. The present study focused on the isolation and purification of lactoferrin of Malabari goats, an indigenous goat b reed of Kerala. Lactoferrin is isolated from colostrum samples by cation exchange chromatography using CM Saphadex C-50 column. The isolated protein was identified and confirmed by SDS-PAGE in terms of its molecular weight. A single 80 kDa Coomassie Brilliant Blue-stained band observed in the electrophoretic profile ascertained the purity of the protein isolated. The results of the study point to a simple one step method to obtain pure lactoferrin from goats.

show abstract

Isolation, Purification and Characterization of Lactoferrin from Goat Colostrum Whey

Cited by 6 publications

References 32 publications

Prospects of lactoferrin as potential natural antibiotic

Prospects of lactoferrin as potential natural antibiotic

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

Isolation and purification of lactoferrin from colostrum of Malabari goats

Contact Info

Product

Resources

About