Selective Catalytic Esterification of Biomass-Based Emulsion Gels by Multi-scale Immobilized Enzymes
摘要
Emulsion gels are important substitutes for saturated fats in the development of health food. However, the stability, oil content, and oil holding capacity of emulsion gels obtained by conventional octenyl succinic anhydride–modified sodium alginate complex with soybean protein are inadequate for solid fat replacement. In this study, a spatially selective catalytic strategy based on lipase-inorganic metal immobilized enzyme is utilized to obtain octenyl succinic anhydride–modified sodium alginate with a concentrated distribution of hydrophobic groups. The amphiphilic sodium alginate with concentrated hydrophobic groups, obtained via this spatially selective catalytic strategy, markedly reduced the mean droplet diameter (704.13 ± 139 nm) compared to that of the conventional chemical modification, resulting in an approximately 41.36% decrease in our experiments. This improved emulsifying performance, characterized by reduced droplet size and enhanced oil–water interfacial stability, subsequently contributed to a more uniform and stable three-dimensional network in the modified sodium alginate-soybean protein composite emulsion gel. Consequently, compared with gels prepared using conventionally chemically modified sodium alginate, the resulting gels exhibited significantly higher oil content (50.51 ± 0.42% w/w) and oil holding capacity (91 ± 0.19%), with increases of 61.49% and 64.12%, respectively. Furthermore, the cyclic compression hysteresis behavior of the obtained emulsion gels (dissipated energy ratio 4.15 ± 0.03) is very analogous to real fat (pork fat dissipated energy ratio 3.47 ± 0.05).