Formation and in vitro starch digestibility of amylose-lipid complex using cooked rice starch and an emulsified formulation.

This study aimed to investigate amylose-lipid complex (ALC) formation and starch digestibility in cooked rice starches (CRSs) with the addition of 0, 5, and 10 % emulsified formulation (EMF). The addition of EMF did not affect the content of non-starch lipids but tended to increase the content of total lipids and starch lipids. The absorption rate of 995 cm/1022 cm of CRSs increased with the addition of EMF, while that of 1047 cm/1022 cm remained unchanged regardless of the addition of EMF.

Structural characteristics determining starch digestibility in cooked rice complexed with an emulsion formulation.

To evaluate the effects of structural characteristics on amylose-lipid complex (ALC) formation and the starch digestibility of cooked rice grains with the addition of 0, 5, 10, and 20 % emulsification formulation (EMF), both cooked rice (CR) grains with intact structural characteristics and CR slurries with their structural characteristics destroyed were examined. When EMF was added, the surface firmness, adhesiveness and adhesion of the CR grain changed. Depressions associated with ALC formation were observed on the surface of CR grains.

Assessing the Postprandial Glycemic Response to Japonica Rice (Oryza sativa L. cv. Koshihikari) with a Small Amount of Lysolecithin and Canola Oil in Japanese Adult Men: a Double-blind, Placebo-controlled, Crossover Study.

A double-blind, placebo-controlled, crossover trial was performed to analyze the effects of a small amount of lysolecithin and canola oil on blood glucose levels after consuming japonica rice. Overall, 17 Japanese adult men were assigned to consume 150 g of normally cooked japonica rice (placebo group) and 150 g of japonica rice cooked with 18 mg of lysolecithin and 1.8 g of canola oil (treatment group); these lipids were added as emulsified formulation (EMF) for stability and uniformity.

Molecular characterization of the protease from Clostridium botulinum serotype C responsible for nicking in botulinum neurotoxin complex.

A protease was purified from the culture medium of Clostridium botulinum serotype C strain Stockholm (C-St). The purified protease belonged to the cysteine protease family based on assays for enzyme inhibitors, activators and kinetic parameters. The protease formed a binary complex consisting of 41- and 17-kDa proteins held together non-covalently.

Clostridium botulinum serotype D neurotoxin and toxin complex bind to bovine aortic endothelial cells via sialic acid.

Botulinum neurotoxin (BoNT) is produced as a large toxin complex (L-TC) associated with nontoxic nonhemagglutinin (NTNHA) and three hemagglutinin subcomponents (HA-70, -33 and -17). The binding properties of BoNT to neurons and L-TC to intestinal epithelial cells are well documented, while those to other tissues are largely unknown. Here, to obtain novel insights into the pathogenesis of foodborne botulism, we examine whether botulinum toxins bind to vascular endothelial cells.