Silkworm pupa protein isolate (SPPI) is rich in amino acids, making it chemically reactive, degradable, and easy to form lysinoalanine (LAL). We investigated how conformational cross-linking, induced by ultrasound-assisted sodium alginate, could inhibit the formation of LAL during the preparation of SPPI. Glycoconjugated SPPI (using 1 % sodium alginate under ultrasonication) showed the lowest LAL content i.e., 7.403 μg·mg-1, representing a 49.58 % decrease, with reference to the control. The ionic, hydrogen, and covalent bonds in the glycoconjugate increased by 171.79 %, 8.48 %, and 35.56 %, respectively. Glycation decreased arginine by 28.92 % and caused the oxidation of tyrosine, methionine and proline to form carbonyl groups. Some precursor amino acids, including lysine, serine, cysteine and threonine were not degraded during the combined treatment. The macromolecular aggregation caused by structural modifications strengthened the steric resistance of LAL cross-linking. The study outcomes provide a novel approach and theoretical basis for inhibition of LAL formation in SPPI.
Keywords: Amino acid; Correlational analysis; Insect protein; Lysinoalanine; Polysaccharide; Ultrasonication.
Copyright © 2024 Elsevier Ltd. All rights reserved.