Low immunoreactive glycated soybean antigen proteins production: system-wide analysis of their immunogenicityin vitroandin vivo

Abstract

The current study aimed to remit the immunoreactivity of glycinin and β-conglycinin through the methods of glycation. The immunoreactivity of the glycated soybean antigen proteins after hydrolyzed was analyzed in vitro. Then in the in vivo trial, 24 crossbred castrated piglets were allocated to four dietary treatments in a complete block design, each treatment with six replicates. From day 29-43, the control groups were fed diets with 4% unglycated glycinin or β-conglycinin, while the treatment groups received diets containing 4% glycated glycinin or β-conglycinin. Generally, the immunoreactivity removal rate increased in all products as time went on both in vitro and in vivo. The immunoreactivity residual rate of unglycated soybean antigen protein was much higher than those of the glycated ones in vitro. Moreover, pepsin and trypsin affected glycated glycinin and glycated β-conglycinin in a different way.

Dietary soybean β‐conglycinin suppresses growth performance and inconsistently triggers apoptosis in the intestine of juvenile grass carp ( Ctenopharyngodon idella ) in association with ROS‐mediated MAPK signalling

“…First, the different effects may be associated with β‐conglycinin itself. β‐Conglycinin is an immunogenic glycoprotein (Wang, Tan, & Sun, ) that possesses the potential to activate NOX (Brandes et al, ). The indigestibility of β‐conglycinin determines its various digestion products produced along the different intestinal segments of rats (Perez, Mills, Lambert, Johnson, & Morgan, ).…”

“…Notably, in the current study, ROS played a pivotal role in dietary β-conglycinin-induced apoptosis among the different intestinal segments in the juvenile grass carp. In organisms, the ROS concentration is primarily determined by ROS generation (Holmström & Finkel, 2014 (Wang, Tan, & Sun, 2015) that possesses the potential to activate NOX (Brandes et al, 2014). The indigestibility of β-conglycinin determines its various digestion products produced along the different intestinal segments of rats (Perez, Mills, Lambert, Johnson, & Morgan, 2000).…”