Hostname: page-component-cd9895bd7-jkksz Total loading time: 0 Render date: 2024-12-18T16:02:12.327Z Has data issue: false hasContentIssue false
  • English
  • Français

Protein secondary structures (α-helix and β-sheet) at a cellular level and protein fractions in relation to rumen degradation behaviours of protein: a new approach

Published online by Cambridge University Press:  08 March 2007

Peiqiang Yu
Peiqiang Yu*
Affiliation:
Department of Animal and Poultry Science, University of Saskatchewan, 51 Campus Drive, Saskatoon SK, Canada S7N 5A8
*
*Corresponding author: Dr Peiqiang Yu, fax 306 966 4151, email [email protected]
Rights & Permissions [Opens in a new window]

Abstract

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

Studying the secondary structure of proteins leads to an understanding of the components that make up a whole protein, and such an understanding of the structure of the whole protein is often vital to understanding its digestive behaviour and nutritive value in animals. The main protein secondary structures are the α-helix and β-sheet. The percentage of these two structures in protein secondary structures influences protein nutritive value, quality and digestive behaviour. A high percentage of β-sheet structure may partly cause a low access to gastrointestinal digestive enzymes, which results in a low protein value. The objectives of the present study were to use advanced synchrotron-based Fourier transform IR (S-FTIR) microspectroscopy as a new approach to reveal the molecular chemistry of the protein secondary structures of feed tissues affected by heat-processing within intact tissue at a cellular level, and to quantify protein secondary structures using multicomponent peak modelling Gaussian and Lorentzian methods, in relation to protein digestive behaviours and nutritive value in the rumen, which was determined using the Cornell Net Carbohydrate Protein System. The synchrotron-based molecular chemistry research experiment was performed at the National Synchrotron Light Source at Brookhaven National Laboratory, US Department of Energy. The results showed that, with S-FTIR microspectroscopy, the molecular chemistry, ultrastructural chemical make-up and nutritive characteristics could be revealed at a high ultraspatial resolution (∼10 μm). S-FTIR microspectroscopy revealed that the secondary structure of protein differed between raw and roasted golden flaxseeds in terms of the percentages and ratio of α-helixes and β-sheets in the mid-IR range at the cellular level. By using multicomponent peak modelling, the results show that the roasting reduced (P<0·05) the percentage of α-helixes (from 47·1 % to 36·1 %: S-FTIR absorption intensity), increased the percentage of β-sheets (from 37·2 % to 49·8 %: S-FTIR absorption intensity) and reduced the α-helix to β-sheet ratio (from 0·3 to 0·7) in the golden flaxseeds, which indicated a negative effect of the roasting on protein values, utilisation and bioavailability. These results were proved by the Cornell Net Carbohydrate Protein System in situ animal trial, which also revealed that roasting increased the amount of protein bound to lignin, and well as of the Maillard reaction protein (both of which are poorly used by ruminants), and increased the level of indigestible and undegradable protein in ruminants. The present results demonstrate the potential of highly spatially resolved synchrotron-based infrared microspectroscopy to locate ‘pure’ protein in feed tissues, and reveal protein secondary structures and digestive behaviour, making a significant step forward in and an important contribution to protein nutritional research. Further study is needed to determine the sensitivities of protein secondary structures to various heat-processing conditions, and to quantify the relationship between protein secondary structures and the nutrient availability and digestive behaviour of various protein sources. Information from the present study arising from the synchrotron-based IR probing of the protein secondary structures of protein sources at the cellular level will be valuable as a guide to maintaining protein quality and predicting digestive behaviours.

Keywords

Synchrotron-based FTIR microspectroscopyFeed molecular chemistryProtein secondary structuresα-Helixβ-SheetProtein nutritive valueDigestive behaviourProtein fractions
Type
Research Article
Information
British Journal of Nutrition , Volume 94 , Issue 5 , November 2005 , pp. 655 - 665
Copyright
Copyright © The Nutrition Society 2005

References

Association of Official Analytical Chemists (1990) Official Methods of Analysis, 15th edn. Arlington, VA: AOAC.Google Scholar
Budevska, BO (2002) In Handbook of Vibrational Spectroscopy, vol. 5. Applications of Vibrational Spectroscopy in Life, Pharmaceutical and Natural Sciences, pp. 3720–3732. (Chalmers, JM and Griffiths, PR, editors). New York: John Wiley and Sons, Inc.Google Scholar
Carey, FA (1996) Organic Chemistry, 3rd edn. New York: McGraw-Hill.Google Scholar
Chalupa, W & Sniffen, CJ (1994) Carbohydrate, protein and amino acid nutrition of lactating dairy cattle. In Recent Advances in Animal Nutrition, pp. 265–275 (Garnsworty, PC & Wiseman, J, editors) Loughborough: Nottingham University Press.Google Scholar
Chandler, NJ (2003) Dairy Cattle – Feather meal: its nutritional value and use in dairy and beef rations. http://www.engormix.com/e_articles_dairy_cattle.asp?ID=79 (November 2003)/Google Scholar
Chaudhry, AS & Webster, AJF (1993) The true digestibility and biological value for rats of undegraded dietary nitrogen in feeds for ruminant. Anim Feed Sci Technol 42, 209–221.CrossRefGoogle Scholar
Dumas, P (2003) Synchrotron IR microspectroscopy: a multidisciplinary analytical technique. Sixth Annual Synchrotron CLS Users’ Meeting and Associated Synchrotron Workshops – WinXAS and Infrared.University of Saskatchewan,Canada,13–15 November.Google Scholar
Dyson, HJ & Wright, PE (1990) Peptide conformation and protein folding. Curr Opin Struct Biol 3, 60–65.CrossRefGoogle Scholar
Elizalde, JC, Merchen, NR & Faulkner, DB (1999) Fractionation of fiber and crude protein in fresh forages during the spring growth. J Anim Sci 77, 476–484.CrossRefGoogle ScholarPubMed
Fraser, RDB, MacCrae, TP & Rogers, GE (1972) Keratins. Springheld, USA: Charles C Thomas.Google Scholar
Goelema, JO (1999) Processing of legume seeds: effect on digestive behaviours in dairy cows. PhD Thesis, Wageningen Agricultural University, The Netherlands.Google Scholar
Greg, K & Rogers, GE (1986) Feather keratin: composition, structure and biogenesis. In Biology of Integuments, vol. 2. Heidelberg: Springer Verlag.Google Scholar
Griffiths, PR & Pariente, G (1986) Trends in analytical chemistry. In Introduction to Spectral Deconvolution, vol. 5, pp. 209. Amsterdam, Netherlands: Elsevier.Google Scholar
Himmelsbach, DS, Khalili, S & Akin, DE (1998) FT-IR microspectroscopic imaging of flax ( Linum usitatissimum L.) stems. Cell Mol Biol 44, 99–108.Google ScholarPubMed
Holman, Hoi-Ying N, Bjornstad, KA, McNamara, MP, Martin, MC, McKinney, WR & Blakely, EA (2002) Synchrotron infrared spectromicroscopy as a novel bioanalytical microprobe for individual living cells: cytotoxicity considerations. J Biomed Optics 7, 1–10.CrossRefGoogle ScholarPubMed
Holum, JR (1982) Fundamentals of General, Organic, and Biological Chemistry, 2nd edn. New York: J Wiley & Sons.Google Scholar
Jackson, M & Mantsch, HH (2000) Infrared spectroscopy ex vivo tissue analysis. In Encyclopedia of Analytical Chemistry, pp. 1–20 (Meyers, L, ed.). Chichester: John Wiley and Sons Ltd.Google Scholar
Kauppinen, JK, Moffatt, DJ, Mantsch, HH & Cameron, DG (1981) Fourier selfdeconvolution: a method for resolving intrinsically overlapped bands. Appl Spectroscy 35, 271–276.CrossRefGoogle Scholar
Kemp, W (1991) Organic Spectroscopy, 3rd edn., New York: WH Freeman.CrossRefGoogle Scholar
Licitra, G, Hernandez, TM & Van Soest, PJ (1996) Standardization of procedures for nitrogen fractionation of ruminant feeds. Anim Feed Sci Technol 57, 347–358.CrossRefGoogle Scholar
Mantsch, HH & Chapman, D (1996) Infrared Spectroscopy of Biomolecules. New York: John Wiley & Sons.Google Scholar
Marinkovic, NS, Huang, R, Bromberg, P et al. (2002) Center for Synchrotron Biosciences’ U2B beamline: an international resource for biological infrared spectroscopy. J Synchrotron Radiat 9, 189–197.CrossRefGoogle ScholarPubMed
Martin, MC (2002) Fourier-transform infrared spectroscopy. http://www.nsls.bnc-gov/newsroom/publications/otherpubs/imaging0502/workshopmillerhighres.pdf (accessed 7 Sep 2005).Google Scholar
Miller, LM (2000) The impact of infrared synchrotron radiation on biology: past, present, and future. Synchrotron RadiatNews 13, 31–37.CrossRefGoogle Scholar
Miller, LM (2002) Infrared microspectroscopy and imaging. http://www.nsls.bnl- gov/newsroom/publications/otherpubs/imaging0502/workshopmillerhighres.pdf(accessed7sep05)Google Scholar
National Research Council (1996) Nutrient Requirement of Beef Cattle, 7th edn. Washington, DC: National Academy Press.Google Scholar
National Research Council (2001) Nutrient Requirement of Dairy Cattle, 7th edn. Washington, DC: National Academy Press.Google Scholar
Rebolé, A, Treviño, J, Caballero, R & Alzueta, C (2001) Effect of maturity on the amino acid profiles of total and nitrogen fractions in common vetch forage. J Sci Food Agric 81, 455–461.3.0.CO;2-V>CrossRefGoogle Scholar
SAS (1998) User's Guide: Statistics, 8th edn., Cary, NC: SAS Institute.Google Scholar
Seguchi, M, Takemoto, M, Mizutani, U, Ozawa, M, Nakamura, C & Matsumura, Y (2004) Effects of secondary structures of heated egg white protein on the binding between prime starch and tailings fractions in fresh wheat flour. Cereal Chem 81, 633–636.CrossRefGoogle Scholar
Sniffen, CJ, O'Connor, JD, Van Soest, PJ, Fox, DG & Russell, JB (1992) A net carbohydrate and protein system for evaluating cattle diets. II. Carbohydrate and protein availability. J Anim Sci 70, 3562–3577.CrossRefGoogle ScholarPubMed
Soita, HW, Meier, JA, Fehr, M, Yu, P, Christensen, DA, McKinnon, JJ & Mustafa, AF (2003) Effects of flaxseed supplementation on milk production, milk fatty acid composition and nutrient utilization by lactating dairy cows. Arch Anim Nutr 57, 107–116.CrossRefGoogle ScholarPubMed
Stewart, D, McDougall, GJ & Baty, A (1995) Fourier transform infrared microspectroscopy of anatomically different cells of falx ( Linum usitatissimum ) stems during development. J Agric Food Chem 43, 1853–1858.CrossRefGoogle Scholar
Van der Poel, AFB, Blonk, J, Van Zuilichem, DJ & Van Oort, MG (1990) Thermal inactivation of lectins and trypsin inhibitor activity during steam processing of dry beans ( Phaseolus vulgaris ) and effects on protein quality. J Sci Food Agric 53, 215–228.CrossRefGoogle Scholar
Van Soest, PJ, Robertson, JB & Lewis, BA (1991) Symposium: Carbohydrate methodology, metabolism and nutritional implications in dairy cattle. Methods for dietary fiber, neutral detergent fiber and non-starch polysaccharides in relation to animal nutrition. J Dairy Sci 74, 3583–3597.CrossRefGoogle Scholar
Ward Lundgren, HP (1954) Formation, composition and properties of keratins. Adv Protein Chem 9, 244–297.Google Scholar
Weiss, WP, Conrad, HR & Pierre, NS (1992) A theoretically based model for predicting total digestible nutrient values of forages and concentrates. Anim Feed Sci Technol 39, 95–110.CrossRefGoogle Scholar
Wetzel, DL (2001) When molecular causes of wheat quality are known, molecular methods will supercede traditional methods. Proceedings of the Second International Wheat Quality Conference, Manhattan, Kansas, USA, May. 2001.Google Scholar
Wetzel, DL, Eilert, AJ, Pietrzak, LN, Miller, SS & Sweat, JA (1998) Ultraspatially resolved synchrotron infrared microspectroscopy of plant tissue in situ. Cell Mol Biol 44, 145–167.Google ScholarPubMed
Wetzel, DL, Srivarin, P & Finney, JR (2003) Revealing protein infrared spectral detail in a heterogeneous matrix dominated by starch. Vib Spectrosc 31, 109–114.CrossRefGoogle Scholar
Yu, P (2004) Application of advanced synchrotron-based Fourier transform infrared microspectroscopy (SR-FTIR) to animal nutrition and feed science: a novel approach. Br J Nutr 92, 869–885.CrossRefGoogle Scholar
Yu, P, Goelema, JO, Leury, BJ, Tamminga, S & Egan, AR (2002) An analysis of the nutritive value of heat processed legume seeds for animal production using the DVE/OEB model: a review [Scientific review article]. Anim Feed Sci Technol 99, 141–176.CrossRefGoogle Scholar
Yu, P, McKinnon, JJ, Christensen, CR, & Christensen, DA (2003. a ) Mapping plant composition with synchrotron infrared microspectroscopy and relation to animal nutrient utilization [Invited article and conference speech]. Proceedings of the Canadian Society of Animal Science Conference, University of Saskatchewan, Saskatoon, Canada, 10–13 June.Google Scholar
Yu, P, McKinnon, JJ, Christensen, CR, Christensen, DA, Marinkovic, NS & Miller, LM (2003b) Chemical imaging of micro-structures of plant tissues within cellular dimension using synchrotron infrared microspectroscopy. J Agric Food Chem 51, 6062–6067.CrossRefGoogle Scholar
Yu, P, McKinnon, JJ, Christensen, CR & Christensen, DA (2004a) Using synchrotron-based FTIR microspectroscopy to reveal chemical features of feather protein secondary structure: comparison with other feed protein sources. J Agric Food Chem 52, 7353–7361.CrossRefGoogle ScholarPubMed
Yu, P, Tamminga, S, Egan, AR & Christensen, DA (2004b) Probing equivocal effects of heat processing of legume seeds on performance of ruminants – a review [Scientific review article]. Asian Austr J Anim Sci 17, 869–876.CrossRefGoogle Scholar
Yu, P, Christensen, DA, Christensen, CR, Drew, MD, Rossnagel, BG & McKinnon, JJ (2004c) Use of synchrotron FTIR microspectroscopy to identify chemical differences in barley endosperm tissue in relation to rumen degradation characteristics. Can J Anim Sci 84, 523–527.CrossRefGoogle Scholar
Yu, P, McKinnon, JJ, Christensen, DA & Christensen, CR (2004d) Applications of synchrotron technology (SR–FTIR) to feed analysis and utilization: a novel approach [Conference article]. Proceedings of the 25th Western Nutrition Conference, Nutrient Requirement and Ingredient Evaluation in the 21st Century.Saskatoon, Canada,28–30 September.Google Scholar
Yu, P, McKinnon, JJ, Christensen, CR & Christensen, DA (2004e) Using synchrotron transmission FTIR microspectroscopy as a rapid, direct and non-destructive analytical technique to reveal molecular microstructural-chemical features within tissue in grain barley. J Agric Food Chem 52, 1484–1494.CrossRefGoogle Scholar
Yu, P, McKinnon, JJ, Christensen, CR & Christensen, DA (2004f) Imaging molecular chemistry of Pioneer corn. J Agric Food Chem 52, 7345–7352.CrossRefGoogle ScholarPubMed
Yu, P, Christensen, DA, McKinnon, JJ & Soita, HW (2004g) Using chemical and biological approaches to predict energy values of selected forages affected by variety and maturity stage. Asian Austr J Anim Sci 17, 228–236.CrossRefGoogle Scholar
Yu, P (2005 a ) Using synchrotron infrared microspectroscopy to reveal microstructural-chemical features of feed/food/plant tissues at a cellular and subcellular level [Invited conference article and speech]. 96th American Oil Chemists Society Annual Conference and Expo,Salt Lake City, Utah, USA,1–4 May.Google Scholar
Yu, P (2005b) Application of cluster analysis (CLA) in feed chemical imaging to accurately reveal structural-chemical features of feeds within cellular dimension. J Agric Food Chem 53, 2872–2880.CrossRefGoogle ScholarPubMed