Impacts of yeast β‐glucan on thermal aggregation and flavour adsorption capacity of Spanish mackerel myosin

Abstract

SummaryThe effects of yeast β‐glucan (YG) on the aggregation and flavour adsorption capacity of Spanish mackerel myosin under two‐step heat treatments were investigated. The surface hydrophobicity and active sulfhydryl content of heat‐induced myosin was increased by the addition of YG, reaching the maximum values of 81.46 and 17.49 mol per 105 g after heating at 90 °C for 10 min. YG incorporation significantly decreased the α‐helix content of myosin to the minimum value of 48.27%, whereas the β‐sheet was increased. The addition of YG promoted the unfolding of myosin, exposing more hydrophobic bonding sites, thus enhancing the flavour‐binding capacity of myosin. Lengthy heating at 90 °C combined with YG addition accelerated the cross‐linking and aggregation of myosin, leading to the re‐embedding of the exposed hydrophobic groups as much as the reduction of flavour‐binding sites. However, YG's unique porous structure could also boost the flavour adsorption ability of myosin containing YG.