Protein Molecular Structures, Protein SubFractions, and Protein Availability Affected by Heat Processing: A Review

Abstract


 The utilization and availability of protein depended on the types of protein and their specific susceptibility to enzymatic hydrolysis (inhibitory activities) in the gastrointestine and was highly associated with protein molecular structures. Studying internal protein structure and protein subfraction profiles leaded to an understanding of the components that make up a whole protein. An understanding of the molecular structure of the whole protein was often vital to understanding its digestive behavior and nutritive value in animals. In this review, recently obtained information on protein molecular structural effects of heat processing was reviewed, in relation to protein characteristics affecting digestive behavior and nutrient utilization and availability. The emphasis of this review was on (1) using the newly advanced synchrotron technology (S-FTIR) as a novel approach to reveal protein molecular chemistry affected by heat processing within intact plant tissues; (2) revealing the effects of heat processing on the profile changes of protein subfractions associated with digestive behaviors and kinetics manipulated by heat processing; (3) prediction of the changes of protein availability and supply after heat processing, using the advanced DVE/OEB and NRC-2001 models, and (4) obtaining information on optimal processing conditions of protein as intestinal protein source to achieve target values for potential high net absorbable protein in the small intestine. The information described in this article may give better insight in the mechanisms involved and the intrinsic protein molecular structural changes occurring upon processing

Effect of protein secondary structures in mixed feedstuff detected by Fourier transform infrared spectroscopy on ruminal protein degradation kinetics

“…Each biological component has a unique molecular structural feature, thus each has its own unique infrared spectrum (Yu 2007). Protein has a unique molecular structure, so it has its own infrared spectrum (Krimm and Bandekar 1986).…”

“…To date, some results on protein molecular structures in relation to nutritive value, digestive behaviours, and availability of protein in animals have been reported for single feedstuff (Yu 2004(Yu , 2007Yu et al 2004;Liu et al 2015). But fewer reports have been found for mixed feedstuff, using S-FTIR or globar-sourced FTIR.…”

“…So, chemical analysis fails to reveal protein internal structure and link protein molecular structural information to chemical and nutritional availability (Budevska 2002;Yu 2004). Published results showed that plant protein nutritive quality and availability were closely related not only to total protein and ruminal degraded behaviours, but also to their inherent protein molecular structure Yu 2007).…”

Effects of Dietary Supplementation with Pumpkin oil (Cucurbita pepo) on Performance and Blood Fat of Broiler Chickens during Finisher Period

“…Even two plants have the same total chemical composition, if inherent structures different, the nutritive values are different. For example, Harrington barley and Valier barley which are similar in chemical composition, but digestive behavior and nutrient availability are completely different (Yu, 2007). Nowadays, Wheat Germ Agglutinin (WGA), Peanut Agglutinin (PNA) and Concavilin (Cona) are being used widely for studying sugar compounds on the surface of cells (Yazdani Moghaddam et al, 2009).…”

Researching rumen degradation behaviour of protein by FTIR spectroscopy

“…These spectral features could be used to explain protein molecular structure makeup and to predict protein supply (Doiron et al 2009;Yu et al 2011). According to recent reports, the newly advanced synchrotron-based Fourier transform infrared microspectroscopy (S-FTIR) is a rapid, direct, non-invasive, and nondestructive bioanalytical technique (Wetzel et al doi: 10.17221/7908-CJAS 1998), and applicable in revealing protein structural features at a cellular level (Yu et al 2004a,b) and protein molecular chemistry affected by heat processing within intact plant tissues (Yu 2007). In general, globar-sourced FTIR (G-FTIR) works with globar-source light, however, light for S-FTIR is provided from a synchrotron source.…”