The Role and Isolation Techniques of Breast Milk Folate Binding Protein

Subandrate Subandrate, M. Irsan Saleh, Dwirini Retno Gunarti, Hermansyah Hermansyah, Mohamad Sadikin

Abstract


Breast milk folate binding protein has a different structure and molecular weight from cow's milk folate binding protein.  The technique of isolation and purification of folate binding protein from various samples is different. This review discusses the structure, role, and isolation techniques of breast milk folate binding protein. This is a systematic literature review created by collecting literature from ScienceDirect, PubMed, Directory of Open Access Journals, and Google Scholars. The keywords used are "folate binding protein" or "folate receptor". The research was conducted from January to July 2024. Breast milk folate binding protein consists of 255-257 amino acids, 4 carbohydrate groups and 16 disulfide bridges. The sequence alignment of amino acid between breast milk and cow's milk folate binding protein is 74.09%. Folate binding protein plays a role in maintaining the availability of folate by preventing enzymatic digestion, increasing folate absorption, and increasing folate retention. Isolation and purification of cow's milk folate binding protein have been carried out by salting out, dialysis, and 1-2 types of chromatography, while breast milk folate binding protein using polyethylene glycol and 3 types of chromatography. Breast milk folate binding protein has different amino acid sequences from cow's milk folate binding protein. Folate binding protein plays a role in maintaining the availability of folate in breast milk or serum. Folate binding protein can be isolated and purified from breast milk and cow's milk with different techniques. Simple techniques need to be developed to isolate and purify breast milk folate binding protein.

Keywords: Folate binding protein; Isolation techniques, Purification; The role.


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DOI: http://dx.doi.org/10.20527/jstk.v20i2.25397

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Department of Chemistry
Faculty of Mathematics and Natural Sciences
Universitas Lambung Mangkurat
Jl. A. Yani KM. 36 Banjarbaru 70714, Indonesia
Email: [email protected]
ISSN: 1411-1616 E-ISSN: 2549-8215

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