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.
Highlights
Protein and Heat Processing: As we know, protein is one of most important nutrient
By using multi-component peaks modeling at protein amide I region of 1700-1620 cm-1, the results show that the golden contained relatively higher proportions of model-fitted α-helix (47 vs. 37%), lower proportion of model-fitted β-sheet (37 vs. 46%)
Using the synchrotron based analytical technique- synchrotron based FTIR microspectroscopy (S-FTIRM) technique, the results showed that Harrington had a wider range of starch to protein IR absorbance intensity ratio (1.406 to 10.119 vs. 1.419 to 4.274), suggesting that it is more heterogeneous than Valier in endosperm chemical makeup
Summary
Protein and Heat Processing: As we know, protein is one of most important nutrient. Heat processing has been used to improve protein utilization and availability [eg. 1-5] and inactivate antinutrition factors [6] by reducing the solubility of the protein, changing protein subfractions, and reducing rumen fermentation and metabolism, increasing the amounts of protein entering the small intestine for absorption and digestion [1, 5, 7], and reducing rumen conjugated linoleic acid hydrogenation and increasing the amount of conjugated linoleic acid available in the small intestine [8].The mechanism of altering the protein digestive behavior with heat processing, summarized by Goelema [1], involves denaturation (which is a disorganization of the overall molecular shape of a protein), unfolding or uncoiling of a coiled or pleated structure, or the separation of the protein into its subunits, which may unfold or uncoil [9]. Research showed that heat processing affected protein moleclualr structures [10] and changed the protein α-helix to β-sheet ratio [10, 11]. The DVE/OEB system [17, 18] and the NRC-2001 model [19], have been developed based on principles in the existing models or protein evaluation systems, such as PDI [72, 73], ARC [74], NJK-NJF [75], AAT-PVB [76], AP [77], ADPLS and MF [78] These two models consider the strong elements of other developed protein evaluation systems and they introduce new elements, such as the role of energy balance in intestinal protein supply
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