Gelation and microstructural properties of protein hydrolysates from trypsin-treated male gonad of scallop (Patinopecten yessoensis) modified by κ-Carrageenan/K+

This article reported the gelation and microstructural properties of scallop male gonads hydrolysates (SMGHs) in the presence of κ-Carrageenan (κ-C) and treated or untreated with potassium chloride (KCl). The presence of κ-C significantly increased the elastic moduli (10.3–449.5 Pa) and melting temperature (32.7–46.7 °C) of SMGHs. The decrease in the relaxation time (T21, T23) signified the strong binding between SMGHs and κ-C. The blue shift in the amide I and II peals coupled with a new band of 1159 cm−1 in SMGHs/κ-C further demonstrated the electrostatic interactions between SMGHs and κ-C. κ-C rose the percentage of β-sheets from 28.10% to 35.93% but at the expense of α-helix and β-turn fractions and highly ebbed the intrinsic fluorescence of SMGHs. Such scenarios resulted in a more compact network formation and flocculation of κ-C chains. The salt-treatment to κ-C promoted helical formation, however, presence of SMGHs created larger interstitial spaces in the κ-C network due to aggregates of SMGHs and decreased the overall gel strength. The outcome promises novel opportunities in the design and development of functional hydrogels based on protein and polysaccharide complexes for food, pharmaceutical and biomedical applications.