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

• Published in: International journal of biological macromolecules Vol. 175; pp. 422 - 431
• Main Authors: Hui Yan, Tan, Lim, Seng Joe, Babji, Abdul Salam, Rawi, Muhamad Hanif, Sarbini, Shahrul Razid
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.04.2021
• Subjects: EBN hydrolysate; Edible swiftlet's nest; Sialylated-mucin glycopeptide; EBN hydrolysate; Sialylated-mucin glycopeptide; Edible swiftlet's nest
• ISSN: 0141-8130; 1879-0003
• DOI: 10.1016/j.ijbiomac.2021.02.007

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. [Display omitted] •Bioactive ESN hydrolysate is generated by alcalase hydrolysis of ESN SiaMuc-glycoprotein.•Molecular weight of ESN SiaMuc-glycoprotein/peptide decreased with enzymatic hydrolysis.•Effect of alcalase hydrolysis on the molecular weight of ESN after maximized DH is insignificant.•Majority of the ESN SiaMuc-glycoprotein/peptide fractions remain intact after hydrolysis.•Alcalase hydrolyses ESN SiaMuc-glycoprotein with high molecular weight in priority.