Interactions of hsian-tsao polysaccharide with corn starch to reduce its in vitro digestibility.

Hsian-tsao polysaccharide (HP) with preferable bioactivities was used to produce starchy gel foods. This study elucidated how interactions of HP (0-0.6 %, w/v) with gelatinized corn starch (CS, 6 %, w/v) reduced in vitro digestibility of CS. The CS digestibility (82.85 %, without HP) was reduced to 68.85 % (co-heated) and 74.75 % (non-co-heated) when 0.6 % HP was added, demonstrating that HP reduced the CS digestibility to a larger extent under co-heating by both HP-CS interactions and inhibiting digestive enzyme activities by HP which was dominated under non-co-heating. Moreover, when co-heated, HP bonded to the amylose of CS via physical forces with a composite index of 21.95 % (0.4 % HP), impeded CS swelling and promoted CS aggregation with the average particle size increased to 42.95 µm (0.6 % HP). Also, the HP-CS complexes formed strong association network structures that increased their apparent viscosity and digestive fluid viscosity. Additionally, HP enhanced the short-range ordered structure and crystal structure of CS. These results evidenced that HP-CS interactions significantly reduced the CS digestibility by forming physical barriers, viscosity effects, and ordered structures, to hinder the enzymes from accessing starch matrices. This laid a foundation for applying HP to starchy foods with a low predicted glycemic index.

Effects of hsian-tsao polysaccharide on myosin gel structure and its binding capacity to flavor compounds.

Hsian-tsao polysaccharide (HTP) with preferable biological activities was explored to improve the gel qualities of surimi. This study investigated the effects of HTP (0-1.0 mg/mL) on structural changes, in vitro digestibility, and fishy odor binding capacity of heat-induced myosin gels (30 mg/mL). HTP promoted the unfolding of myosin structure with transitions from α- helixes to ß-sheets, accompanied by the enhancement of hydrophobic bonds, hydrogen bonds, and non-disulfide covalent bonds dominated within gel networks. Moreover, HTP facilitated the formation of compact gel structures of myosin with superior elastic properties (G' > G'') and apparent viscosity, but without affecting the final in vitro digestibility. Moreover, the microstructure of gels markedly affected the adsorption rate of flavor compounds, with a lower adsorption rate obtained for myosin-HTP gels with compact gel networks embedded with evenly small cavities. Additionally, HTP affected the flavor-binding capacities of myosin gels by increasing hexanal and heptanal, but reducing nonanal and 1-octen-3-ol, in relation to the combined effects of myosin structural changes and newly formed gel networks. This work provides a new prospect for application of HTP to regulate the adsorption rate and binding capacity of myosin gels to fishy odors, critical for improvement of gel properties in surimi products.