Fractionation and characterisation of sialylated-mucin glycoprotein from edible birds' nest hydrolysates through anion exchange chromatography

Edible bird's nest (EBN) is made up of sialylated-mucin glycoprotein with various health benefits due to its high antioxidative activity. However, as a macromolecule with distinct charged sialic acid and amino acids, fractions with different charges would have varied physicochemical properties...

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Bibliographic Details
Published in:International journal of biological macromolecules 2024-06, Vol.269 (Pt 1), p.132022-132022, Article 132022
Main Authors: Mun, Sue Lian, Ter, Zhi Yin, Ariff, Rafidah Mohd, Rahman, Nur Farhana Abd, Chang, Lee Sin, Latip, Jalifah, Babji, Abdul Salam, Lim, Seng Joe
Format: Article
Language:English
Subjects:
Anion exchange chromatography (AEC)
Antioxidative activity
Edible bird's nest (EBN)
Enzymatic hydrolysate
Fractionation
Sialylated-mucin glycoprotein
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Summary:Edible bird's nest (EBN) is made up of sialylated-mucin glycoprotein with various health benefits due to its high antioxidative activity. However, as a macromolecule with distinct charged sialic acid and amino acids, fractions with different charges would have varied physicochemical properties and antioxidant activity, which have not been studied. Therefore, this study aimed to fractionate and purify the enzymatic hydrolysed of cleaned EBN (EBNhc) and EBN by-product (EBNhbyp) through anion exchange chromatography (AEC), and determine their molecular weights, physicochemical properties, and antioxidative activities. Overall, 26 fractionates were collected from enzymatic hydrolysate by AEC, which were classified into 5 fractions. It was found that the positively charged fraction of EBNhc (CF 1) and EBNhbyp (DF 1) showed the significantly highest (p 
ISSN:0141-8130
1879-0003
DOI:10.1016/j.ijbiomac.2024.132022