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

Mun SL 1 , Ter ZY 1 , Ariff RM 2 , Rahman NFA 3 , Chang LS 4 , Latip J 5 Show all authors , Babji AS 6 , Lim SJ 7

Affiliations 

  • 1 Department of Food Sciences, Faculty of Science and Technology, Universiti Kebangsaan Malaysia, 43600 UKM Bangi, Selangor, Malaysia
  • 2 Department of Food Sciences, Faculty of Science and Technology, Universiti Kebangsaan Malaysia, 43600 UKM Bangi, Selangor, Malaysia; International Institute for Halal Research and Training (INHART), International Islamic University Malaysia (IIUM), 53100 Jalan Gombak, Selangor, Malaysia
  • 3 School of Industrial Technology, Faculty of Applied Sciences, Universiti Teknologi MARA, UiTM Shah Alam, Shah Alam 40450, Selangor, Malaysia
  • 4 Department of Food Science and Nutrition, Faculty of Applied Sciences, UCSI University Kuala Lumpur, No.1, Jalan Menara Gading, UCSI Heights 56000 Cheras, Kuala Lumpur, Malaysia; Innovation Centre for Confectionery Technology (MANIS), Faculty of Science and Technology, Universiti Kebangsaan Malaysia, 43600 UKM Bangi, Selangor, Malaysia. Electronic address: leesin@ukm.edu.my
  • 5 Department of Chemical Sciences, Faculty of Science and Technology, Universiti Kebangsaan Malaysia, 43600 UKM Bangi, Selangor, Malaysia. Electronic address: jalifah@ukm.edu.my
  • 6 Department of Food Sciences, Faculty of Science and Technology, Universiti Kebangsaan Malaysia, 43600 UKM Bangi, Selangor, Malaysia; Innovation Centre for Confectionery Technology (MANIS), Faculty of Science and Technology, Universiti Kebangsaan Malaysia, 43600 UKM Bangi, Selangor, Malaysia. Electronic address: daging@ukm.edu.my
  • 7 Department of Food Sciences, Faculty of Science and Technology, Universiti Kebangsaan Malaysia, 43600 UKM Bangi, Selangor, Malaysia; Innovation Centre for Confectionery Technology (MANIS), Faculty of Science and Technology, Universiti Kebangsaan Malaysia, 43600 UKM Bangi, Selangor, Malaysia. Electronic address: joe@ukm.edu.my
Int J Biol Macromol, 2024 May 01;269(Pt 1):132022.
PMID: 38697414 DOI: 10.1016/j.ijbiomac.2024.132022

Abstract

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 

* Title and MeSH Headings from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Similar publications