Work

Identification and comparison of N-glycome profiles from common dietary protein sources

Year: 2024

Type: article

Abstract: The N- glycomes of bovine whey, egg white, pea, and soy protein isolates are described here. N -glycans from four protein isolates were analyzed by HILIC high performance liquid chromatography and quadrupole time-of-flight tandem mass spectrometry (HILIC-FLD-QTOF-MS/MS). In total, 33 N- glycans from bovine whey and egg white and 10 N -glycans from soy and pea glycoproteins were identified. The type of N- glycans per glycoprotein source were attributable to differences in biosynthetic glycosylation pathways. Animal glycoprotein sources favored a combination of complex and hybrid glycan configurations, while the plant proteins were dominated by oligomannosidic N -glycans. Bovine whey glycoprotein isolate contained the most diverse N- glycans by monosaccharide composition as well as structure, while plant sources such as pea and soy glycoprotein isolates contained an overlap of oligomannosidic N- glycans. The results suggest N- glycan structure and composition is dependent on the host organism which are driven by the differences in N- glycan biosynthetic pathways. • N -glycans are common among dietary protein sources. • Similarities in the biosynthesis of N -glycans shapes the overall N -glycome. • Plant sourced protein (soybean and pea) share many of their N -glycan structures. • The N -glycome from egg white and bovine whey were compositionally more distinct due to greater variation of monosaccharides.

Source: Food Chemistry X

DOI: 10.1016/j.fochx.2024.102025