Enzymatic hydrolysis: Sialylated mucin (SiaMuc) glycoprotein of edible swiftlet's nest (ESN) and its molecular weight distribution as bioactive ESN SiaMuc-glycopeptide hydrolysate

Hui Yan T 1 , Lim SJ 2 , Babji AS 3 , Rawi MH 4 , Sarbini SR 5

Affiliations 

  • 1 Department of Crop Science, Faculty of Agricultural Science and Forestry, Universiti Putra Malaysia Bintulu Campus, 97008 Bintulu, Sarawak, Malaysia. Electronic address: shyann68huiyan@gmail.com
  • 2 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
  • 3 Innovation Centre for Confectionery Technology (MANIS), Faculty of Science and Technology, Universiti Kebangsaan Malaysia, 43600 UKM Bangi, Selangor, Malaysia; Centre for Innovation and Technology Transfer (INOVASI-UKM), Chancellery, Universiti Kebangsaan Malaysia, 43600 UKM Bangi, Selangor, Malaysia. Electronic address: daging@ukm.edu.my
  • 4 Department of Crop Science, Faculty of Agricultural Science and Forestry, Universiti Putra Malaysia Bintulu Campus, 97008 Bintulu, Sarawak, Malaysia. Electronic address: hanif_rawi@me.com
  • 5 Department of Crop Science, Faculty of Agricultural Science and Forestry, Universiti Putra Malaysia Bintulu Campus, 97008 Bintulu, Sarawak, Malaysia; Halal Products Research Institute, Universiti Putra Malaysia, Putra Infoport, 43400 UPM Serdang, Selangor. Electronic address: shahrulrazid@upm.edu.my
Int J Biol Macromol, 2021 Apr 01;175:422-431.
PMID: 33561458 DOI: 10.1016/j.ijbiomac.2021.02.007

Abstract

Bioactive edible swiftlet's nest (ESN) sialylated-mucin (SiaMuc) hydrolysate is produced by alcalase hydrolysis. Enzymatic hydrolysis of ESN breakdown high-valued ESN SiaMuc-glycoprotein into bioactive SiaMuc-glycopeptide. This is a breakthrough for the issue of insolubility and low extraction rate in ESN, and even increases the bioavailability of ESN nutritional functionality and health benefits. Hydrolysis of ESN SiaMuc-glycoprotein was performed for 1 to 4 h and its effect on physicochemical properties, molecular weight (MW) distribution, SiaMuc-glycoprotein and glycopeptide integrity were determined. Other than improvement in solubility and bioavailability as SiaMuc-glycopeptide, results from SDS-PAGE revealed that MW of SiaMuc-glycoprotein decreased from 42.0-148.8 kDa to 17.7-142.7 kDa with increasing hydrolysis period. Further hydrolysis from maximized DH (90 min) showed an insignificant effect on the MW of ESN SiaMuc-glycopeptide and remained constant at 15.2 kDa. This highlights that enzymatic hydrolysis only influences macro SiaMuc-glycoprotein fractions (142.7, 115.3 and 102.7 kDa), while the majority of SiaMuc-glycopeptide fractions from 36.6-98.6 kDa remained intact. Conclusively, alcalase hydrolysis of ESN showed high recovery in the form of bioactive ESN SiaMuc-glycopeptide. Therefore, enzymatic biotechnology is an economic alternative applicable on ESN that broaden industrial utilization by reducing the MW without destroying the quality of bioactive SiaMuc-glycoprotein.

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

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