RESUMO
Thermal processing with salt ions is widely used for the production of food products (such as whole grain food) containing protein and anthocyanin. To date, it is largely unexplored how salt ion presence during thermal processing regulates the practical performance of protein/anthocyanin binary system. Here, rice albumin (RA) and black rice anthocyanins (BRA) were used to prepare RA/BRA composite systems as a function of temperature (60-100 °C) and NaCl concentration (10-40 mM) or CaCl2 concentration (20 mM). It was revealed that the spontaneous complexing reaction between RA and BRA was driven by hydrophobic interactions and hydrogen bonds and becomes easier and more favorable at a higher temperature (≤90 °C), excessive temperature (100 °C), however, may result in the degradation of BRA. Moreover, the salt ion presence during thermal processing may bind with RA and BRA, respectively, which could restrict the interaction between BRA and RA. Additionally, the inclusion of Na+ or Ca2+ at 20 mM endowed the binary system with strengthened DPPH radical scavenging capacity (0.95 for Na+ and 0.99 for Ca2+). Notably, Ca2+ performed a greater impact on the stability of the system than Na+.
Assuntos
Oryza , Antocianinas , Albuminas , Cloreto de Sódio , Cloreto de Sódio na Dieta , Grão Comestível , ÍonsRESUMO
The suppressive effect of rice albumin (RA) of 16 kDa on elevation of blood glucose level after oral loading of starch or glucose and its possible mechanism were examined. RA suppressed the increase in blood glucose levels in both the oral starch tolerance test and the oral glucose tolerance test. The blood glucose concentrations 15 min after the oral administration of starch were 144 ± 6 mg/dL for control group and 127 ± 4 mg/dL for RA 200 mg/kg BW group, while those after the oral administration of glucose were 157 ± 7 mg/dL for control group and 137 ± 4 mg/dL for RA 200 mg/kg BW group. However, in the intraperitoneal glucose tolerance test, no significant differences in blood glucose level were observed between RA and the control groups, indicating that RA suppresses the glucose absorption from the small intestine. However, RA did not inhibit the activity of mammalian α-amylase. RA was hydrolyzed to an indigestible high-molecular-weight peptide (HMP) of 14 kDa and low-molecular-weight peptides by pepsin and pancreatin. Furthermore, RA suppressed the glucose diffusion rate through a semipermeable membrane like dietary fibers in vitro. Therefore, the indigestible HMP may adsorb glucose and suppress its absorption from the small intestine.