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http://dx.doi.org/10.5713/ajas.15.0701

Relationship between Molecular Structure Characteristics of Feed Proteins and Protein In vitro Digestibility and Solubility  

Bai, Mingmei (Animal Production and Product Quality and Security Key Lab, Ministry of Education, Jilin Agricultural University)
Qin, Guixin (Animal Production and Product Quality and Security Key Lab, Ministry of Education, Jilin Agricultural University)
Sun, Zewei (Animal Production and Product Quality and Security Key Lab, Ministry of Education, Jilin Agricultural University)
Long, Guohui (College of Life Science, Jilin Agricultural University)
Publication Information
Asian-Australasian Journal of Animal Sciences / v.29, no.8, 2016 , pp. 1159-1165 More about this Journal
Abstract
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, corn distiller's dried grains with solubles, corn gluten meal, and feather meal by Fourier transform infrared (FTIR) spectroscopy to determine the protein molecular spectral band characteristics for amides I and II as well as ${\alpha}$-helices and ${\beta}$-sheets and their ratios. Protein solubility and in vitro digestibility were measured with the Kjeldahl method using 0.2% KOH solution and the pepsin-pancreatin two-step enzymatic method, respectively. We found that all measured spectral band intensities (height and area) of feed proteins were correlated with their the in vitro digestibility and solubility ($p{\leq}0.003$); moreover, the relatively quantitative amounts of ${\alpha}$-helices, random coils, and ${\alpha}$-helix to ${\beta}$-sheet ratio in protein secondary structures were positively correlated with protein in vitro digestibility and solubility ($p{\leq}0.004$). On the other hand, the percentage of ${\beta}$-sheet structures was negatively correlated with protein in vitro digestibility (p<0.001) and solubility (p = 0.002). These results demonstrate that the molecular structure characteristics of feed proteins are closely related to their in vitro digestibility at 28 h and solubility. Furthermore, the ${\alpha}$-helix-to-${\beta}$-sheet ratio can be used to predict the nutritional value of feed proteins.
Keywords
Feed; Protein; Protein In vitro Digestibility; Fourier Transform Infrared Spectroscopy; Molecular Structure Characteristics; Protein Solubility;
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1 Adler-Nissen, J. 1979. Determination of the degree of hydrolysis of food protein hydrolysates by trinitro benzene sulfonic acid. J. Agric. Food Chem. 6:1256-1262.
2 AOAC. 1990. Official Methods of Analysis. 15th edn. Association of Official Analytical Chemists, Arlington, VA, USA.
3 Boisen, S. and J. A. Fernandez. 1995. Prediction of the apparent ileal digestibility of protein and amino acids in feedstuffs and feed mixtures for pigs by in vitro analyses. Anim. Feed Sci. Technol. 51:29-43.   DOI
4 Chen, L. M., X. W. Zhang, and P. Q. Yu. 2014. Molecular Spectroscopy Basis to Explore Molecular Structure in Relation to Nutritional Values and Metabolic Characteristics in Dairy Cattle of Chinese DDGS from Different Sources. Ph.D. Tianjin Agricultural University, Tianjin, China.
5 Dale, N. M., M. Araba, and E. Whittle. 1987. Protein solubility as an indicator of optimum processing of soybean meal. In: Proceedings of 1987 Georgia Nutrition Conference for the Feed Industry, Georgia Nutrition Society, Atlanta, GA, USA. pp. 88-95.
6 Doiron, K., P. Yu, J. J. McKinnon, and D. A. Christensen. 2009. Heat-induced protein structure and subfractions in relation to protein degradation kinetics and intestinal availability in dairy cattle. J. Dairy Sci. 92:3319-3330.   DOI
7 Dyson, H. J. and P. E. Wright. 1993. Peptide conformation and protein folding. Curr. Opin. Struct. Biol. 3:60-65.   DOI
8 Huang, R. L., Z. L. Tan, T. X. Xing, Y. F. Pan, and T. J. Li. 2000. An in vitro method for the estimation of ileal crude protein and amino acids digestibility using the dialysis tubing for pig feedstuffs. Anim. Feed Sci. Technol. 88:79-89.   DOI
9 Jiao, P. X., D. S. Liu, S. Zheng, and C. D. Chen. 2012. Study on protein secondary structures on the protein degradability of feeds in rumen of dairy cows. Feed Ind. 33:48-51.
10 Liu, B., P. Thacker, J. McKinnon, and P. Yu. 2013. In-depth study of the protein molecular structures of different types of dried distillers grains with solubles and their relationship to digestive characteristics. J. Sci. Food Agric. 93:1438-1448.   DOI
11 Long, G. H., J. Yuan, H. Pan, Z. Sun, Y. Li, and G. X. Qin. 2015. Characterization of thermal denaturation structure and morphology of soy glycinin by FTIR and SEM. Int. J. Food Prop. 18:763-774.   DOI
12 Meng-Xia, X. and L. Yuan. 2002. Studies on the hydrogen bonding of aniline's derivatives by FT-IR. Spectrochim. Acta A Mol. Biomol. Spectrosc. 58:2817-2826.   DOI
13 Samadi, K. Theodoridou, and P. Yu. 2013. Detect the sensitivity and response of protein molecular structure of whole canola seed (yellow and brown) to different heat processing methods and relation to protein utilization and availability using ATR-FT/IR molecular spectroscopy with chemometrics. Spectrochim. Acta A Mol. Biomol. Spectrosc. 105:304-313.   DOI
14 Papadopoulos, M. C., A. R. El Boushy, A. E. Roodbeen, and E. H. Ketelaars. 1986. Effects of processing time and moisture content on amino acid composition and nitrogen characteristics of feather meal. Anim. Feed Sci. Technol. 14:279-290.   DOI
15 Peng, Q. H., N. A. Khan, Z. Wang, and P. Q. Yu. 2014. Relationship of feeds protein structural makeup in common Prairie feeds with protein solubility, in situ ruminal degradation and intestinal digestibility. Anim. Feed Sci. Technol. 194:58-70.   DOI
16 Qin, G. X., Z. W. Sun, G. H. Long, T. Wang, and M. M. Bai. 2014. The physicochemical property of feedstuff proteins and its effects on the nutritional value. Chin. J. Anim. Nutr. 26:1-7.
17 Tan-Wilson, A. L., P. M. Hartl, N. E. Delfel, and K. A. Wilson. 1985. Differential expression of Kunitz and Bowman-Birk soybean proteinase inhibitors in plant and callus tissue. Plant Physiol. 78:310-314.   DOI
18 Theodoridou, K. and P. Yu. 2013. Application potential of ATR-FT/IR molecular spectroscopy in animal nutrition: Reveal protein molecular structures of canola meal and presscake, as affected by heat processing methods, in relationship with their protein digestive behavior and utilization for dairy cattle. J. Agric. Food Chem. 61:5449-5458.   DOI
19 Xin, H., X. Zhang, and P. Yu. 2013a. Using synchrotron radiation-based infrared microspectroscopy to reveal microchemical structure characterization: frost damaged wheat vs. normal wheat. Int. J. Mol. Sci. 14:16706-16718.   DOI
20 Xin, H., K. C. Falk, and P. Yu. 2013b. Studies on Brassica carinata seed. 1. Protein molecular structure in relation to protein nutritive values and metabolic characteristics. J. Agric. Food Chem. 61:10118-10126.   DOI
21 Yan, X., N. A. Khan, F. Zhang, L. Yang, and P. Yu. 2014. Microwave irradiation induced changes in protein molecular structures of barley grains: relationship to changes in protein chemical profile, protein subfractions, and digestion in dairy cows. J. Agric. Food Chem. 62:6546-6555.   DOI
22 Yu, P., J. J. Mckinnon, C. R. Christensen, and D. A. Christensen. 2004. Using synchrotron-based FTIR micro-spectroscopy to reveal chemical features of feather protein secondary structure: comparison with other feed protein sources. J. Agric. Food Chem. 52:7353-7361.   DOI
23 Yu, P. and W. G. Nuez-Ortin. 2010. Relationship of protein molecular structure to metabolisable proteins in different types of dried distillers grains with solubles: A novel approach. Br. J. Nutr. 104:1429-1437.   DOI
24 Zhang, X. and P. Yu. 2012. Molecular basis of protein structure in combined feeds (hulless barley with bioethanol coproduct of wheat dried distillers grains with solubles) in relation to protein rumen degradation kinetics and intestinal availability in dairy cattle. J. Dairy Sci. 95:3363-3379.   DOI