Poultry by-products and rainbow trout (Onchorhynchus mykiss) viscera are abundant and underutilized resources that can be used as a unique protein source to make protein hydrolysates. In this study protein hydrolysate were made from these two different sources with Alcalase 2.4L. The functional properties of Fish viscera protein hydrolysate (FPH) compared to poultry by-products protein hydrolys...

The nutritional value of feed proteins and their utilization by livestock are related not only to the chemical composition but also to the structure of feed proteins, but few studies thus far have investigated the relationship between the structure of feed proteins and their solubility as well as digestibility in monogastric animals. To address this question we analyzed soybean meal, fish meal,...

Two milk protein concentrates powders with 80% protein content (MPC80) were reconstituted with either water or permeate at 4C or 37C to contain 3.5% protein content. Samples were homogenized at 0 or 13800 kPa. The objective of this research was to determine how different solubility measures such as solubility index, soluble solids and particle size were affected by powder source, reconstitution...

due to the need to find new protein sources with considering the fact that the bitter vetch seed has high levels of protein content, physicochemical and mechanical properties of bitter vetch seed and functional properties of its flour were evaluated in this study. the effects of altering the ph on protein solubility, foaming capacity, foaming stability, emulsion capacity and emulsion stability ...

the use of organophosphorus hydrolase (oph) enzyme to degrade chemical warfare agents is one of the most frequently used decontamination methods. oph is a ~36 kda homodimeric metalloprotein that is found in the membrane of flavobacterium sp. strain atcc 27551 and brevundimonas diminuta mg and is capable of hydrolyzing a wide range of oxon and thion , such as paraoxon and parathion. oph gene ( o...

Protein misfolding resulting in the formation of inclusion bodies is one of the major problems during protein overexpression in Escherichia coil. In this paper, we introduce a new method, which is simply to heat shock a cell culture prior to protein induction, allowing effective enhancement of the solubility and thereby the yield of overexpressed proteins in E. coli. Using this method, we show ...