Hostname: page-component-cd9895bd7-jn8rn Total loading time: 0 Render date: 2024-12-22T18:28:51.193Z Has data issue: false hasContentIssue false
  • English
  • Français

In vitro protein digestion kinetics of protein sources for pigs

Published online by Cambridge University Press:  29 October 2018

H. Chen Open the ORCID record for H. Chen [Opens in a new window] ,
P. A. Wierenga ,
W. H. Hendriks  and
A. J. M. Jansman
H. Chen*
Affiliation:
Animal Nutrition Group, Wageningen University, De Elst 1, 6708WD, Wageningen, The Netherlands Wageningen Livestock Research, De Elst 1, 6708WD, Wageningen, The Netherlands
P. A. Wierenga
Affiliation:
Laboratory of Food Chemistry, Wageningen University, Bornse Weilanden 9, 6708WG, Wageningen, The Netherlands
W. H. Hendriks
Affiliation:
Animal Nutrition Group, Wageningen University, De Elst 1, 6708WD, Wageningen, The Netherlands
A. J. M. Jansman
Affiliation:
Wageningen Livestock Research, De Elst 1, 6708WD, Wageningen, The Netherlands
*
†E-mail: [email protected]
Get access

Abstract

In current feed evaluation systems, the nutritional value of protein sources in diets for pigs is based on the ileal digestibility of protein and amino acids, which does not account for the kinetics of protein digestion along the gastrointestinal tract. The objective of the present study was to determine the in vitro protein digestion kinetics of different protein sources (soya bean meal (SBM), wheat gluten (WG), rapeseed meal (RSM), whey powder (WP), dried porcine plasma protein, yellow meal worm larvae and black soldier fly larvae (BSF)). Protein sources were incubated with pepsin at pH 3.5 for 0 to 90 min and subsequently with pancreatin at pH 6.8 for 0 to 210 min at 39°C. The in vitro protein digestion kinetics were described as the kinetics of nitrogen (N) solubilisation and the release of low molecular weight peptides (LMW) (<500 Da). The N solubilisation rate ranged from 0.025 min−1 for BSF to 0.685 min−1 for WP during the incubation with pepsin, and from 0.027 min−1 for RSM to 0.343 min−1 for WP during the incubation with pancreatin. The release rate of LMW peptides ranged from 0.027 min−1 for WG to 0.093 min−1 for WP during the incubation with pepsin, and from 0.029 min−1 for SBM to 0.385 min−1 for WP. Black soldier fly larvae showed a similar release rate of LMW peptides as WP during the incubation with pancreatin. At the end of the sequential incubation with pepsin (90 min) and pancreatin (210 min), WG and WP showed the highest percentage of N present in LMW peptides relative to total N (78% and 79%, respectively), whereas SBM showed the lowest (35%). In conclusion, protein sources for pig diets show substantial differences in in vitro protein digestion kinetics as measured by the kinetics of N solubilisation and the release of LMW peptides. The rate of release of LMW peptides was not correlated to the rate of N solubilisation for each of the protein sources evaluated.

Keywords

plant protein sourcesporcine plasmayellow meal wormblack soldier fly larvaegastrointestinal protein degradation
Type
Research Article
Information
animal , Volume 13 , Issue 6 , June 2019 , pp. 1154 - 1164
Copyright
© The Animal Consortium 2018 

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Adler-Nissen, J 1976. Enzymic hydrolysis of proteins for increased solubility. Journal of Agricultural and Food Chemistry 24, 1090–1093.Google Scholar
Babinszky, L, van der Meer, JM, Boer, H and Den Hartog, LA 1990. An in-vitro method for prediction of the digestible crude protein content in pig feeds. Journal of the Science of Food and Agriculture 50, 173–178.Google Scholar
Boirie, Y, Dangin, M, Gachon, P, Vasson, MP, Maubois, JL and Beaufrère, B 1997. Slow and fast dietary proteins differently modulate postprandial protein accretion. Proceedings of the National Academy of Sciences 94, 14930–14935.Google Scholar
Boisen, S and Fernández, JA 1995. Prediction of the apparent ileal digestibility of protein and amino acids in feedstuffs and feed mixtures for pigs by in vitro analyses. Animal Feed Science and Technology 51, 29–43.Google Scholar
Bosch, G, Zhang, S, Oonincx, DG and Hendriks, WH 2014. Protein quality of insects as potential ingredients for dog and cat foods. Journal of Nutritional Science 3, e29.Google Scholar
Cone, JW and van der Poel, AFB 1993. Prediction of apparent heal protein digestibility in pigs with a two-step in-vitro method. Journal of the Science of Food and Agriculture 62, 393–400.Google Scholar
Centraal Veevoeder Bureau (CVB) 2016. Chemical compositions and nutritional values of feed ingredients. CVB, Wageningen, The Netherlands.Google Scholar
Dangin, M, Boirie, Y, Garcia-Rodenas, C, Gachon, P, Fauquant, J, Callier, P, Ballèvre, O and Beaufrère, B 2001. The digestion rate of protein is an independent regulating factor of postprandial protein retention. American Journal of Physiology-Endocrinology and Metabolism 280, E340–E348.Google Scholar
Drew, MD, Schafer, TC and Zijlstra, RT 2012. Glycemic index of starch affects nitrogen retention in grower pigs. Journal of Animal Science 90, 1233–1241.Google Scholar
Ganapathy, V, Ganapathy, ME and Leibach, FH 2000. Intestinal transport of peptides and amino acids. Current Topics in Membranes 50, 379–412.Google Scholar
Greenberg, NA and Shipe, WF 1979. Comparison of the abilities of trichloroacetic, picric, sulfosalicylic, and tungstic acids to precipitate protein hydrolysates and proteins. Journal of Food Science 44, 735–737.Google Scholar
Hulshof, TG, van der Poel, AFB, Hendriks, WH and Bikker, P 2016. Processing of soybean meal and 00-rapeseed meal reduces protein digestibility and pig growth performance but does not affect nitrogen solubilization along the small intestine. Journal of Animal Science 94, 2403–2414.Google Scholar
International Organization for Standardization (ISO) 1999a. ISO 6492:1999. Animal feeding stuffs—determination of fat content. ISO, Geneva, Switzerland.Google Scholar
International Organization for Standardization (ISO) 1999b. ISO 6496:1999. Animal feeding stuffs—determination of moisture and other volatile matter content. ISO, Geneva, Switzerland.Google Scholar
International Organization for Standardization (ISO) 2002. ISO 5984:2002. Animal feeding stuffs-determination of crude ash content. ISO, Geneva, Switzerland.Google Scholar
International Organization for Standardization (ISO) 2005. ISO 5983-1:2005. Animal feeding stuffs—determination of N content and calculation of crude protein content—part 1: Kjeldahl method. ISO, Geneva, Switzerland.Google Scholar
International Organization for Standardization (ISO) 2008. ISO 16634-1:2008. Food products—determination of the total N content by combustion according to the Dumas principle and calculation of the crude protein content—Part 1: oilseeds and animal feeding stuffs. ISO, Geneva, Switzerland.Google Scholar
Johnston, SL, Hancock, JD, Hines, RH, Behnke, KC, Kennedy, GA, Maloney, CA, Traylor, SL, Sorrell, SP, Goodband, B and Tokach, M 1998. Effects of expander conditioning of corn-and sorghum-based diets on pellet quality and performance in finishing pigs and lactating sows. In Kansas State University Swine Day 1998. Report of Progress 819, 213–220.Google Scholar
Luo, Q, Boom, RM and Janssen, AE 2015. Digestion of protein and protein gels in simulated gastric environment. LWT-Food Science and Technology 63, 161–168.Google Scholar
Mahé, S, Benamouzig, R, Gaudichon, C, Huneau, JF, de Cruz, I, Rautureau, J and Tomé, D 1995. Nitrogen movements in the upper jejunum lumen in humans fed low amounts of casein or beta-lactoglobulin. Gastroentérologie Clinique et Biologique 19, 20–26.Google Scholar
Malabat, C and Rabiller, C 2001. Emulsifying and foaming properties of native and chemically modified peptides from the 2S and 12S proteins of rapeseed (Brassica napus L.). Journal of the American Oil Chemists’ Society 78, 235–242.Google Scholar
Mangan, J 1988. Nutritional effects of tannins in animal feeds. Nutrition Research Reviews 1, 209–231.Google Scholar
Merchant, HA, McConnell, EL, Liu, F, Ramaswamy, C, Kulkarni, RP, Basit, AW and Murdan, S 2011. Assessment of gastrointestinal pH, fluid and lymphoid tissue in the guinea pig, rabbit and pig, and implications for their use in drug development. European Journal of Pharmaceutical Sciences 42, 3–10.Google Scholar
National Research Council 2012. Nutrient requirements of swine, 11th revised edition. National Academic Press, Washington, DC, USA.Google Scholar
Ørskov, ER and McDonald, I 1979. The estimation of protein degradability in the rumen from incubation measurements weighted according to rate of passage. The Journal of Agricultural Science 92, 499–503.Google Scholar
Picariello, G, Miralles, B, Mamone, G, Sánchez-Rivera, L, Recio, I, Addeo, F and Ferranti, P 2015. Role of intestinal brush border peptidases in the simulated digestion of milk proteins. Molecular Nutrition & Food Research 59, 948–956.Google Scholar
Sánchez-Rivera, L, Ménard, O, Recio, I and Dupont, D 2015. Peptide mapping during dynamic gastric digestion of heated and unheated skimmed milk powder. Food Research International 77, 132–139.Google Scholar
Schwenke, KD, Drescher, B, Zirwer, D and Raab, B 1988. Structural studies on the native and chemically modified low-molecular mass basic storage protein (napin) from rapeseed (Brassica napus L.). Biochemie und Physiologie der Pflanzen 183, 219–224.Google Scholar
Selle, PH, Cowieson, AJ, Cowieson, NP and Ravindran, V 2012. Protein–phytate interactions in pig and poultry nutrition: a reappraisal. Nutrition Research Reviews 25, 1–17.Google Scholar
Silk, DBA, Grimble, GK and Rees, RG 1985. Protein digestion and amino acid and peptide absorption. Proceedings of the Nutrition Society 44, 63–72.Google Scholar
Tonheim, SK, Nordgreen, A, Høgøy, I, Hamre, K and Rønnestad, I 2007. In vitro digestibility of water-soluble and water-insoluble protein fractions of some common fish larval feeds and feed ingredients. Aquaculture 262, 426–435.Google Scholar
van den Borne, JJGC, Schrama, JW, Heetkamp, MJW, Verstegen, MWA and Gerrits, WJJ 2007. Synchronising the availability of amino acids and glucose increases protein retention in pigs. Animal 1, 666–674.Google Scholar
van der Meulen, J, Bakker, JGM, Smits, B and de Visser, H 1997. Effect of source of starch on net portal flux of glucose, lactate, volatile fatty acids and amino acids in the pig. British Journal of Nutrition 78, 533–544.Google Scholar
van der Poel, AFB 1990. Effect of processing on antinutritional factors and protein nutritional value of dry beans (Phaseolus vulgaris L.). A review. Animal Feed Science and Technology 29, 179–208.Google Scholar
van Kempen, TATG, Regmi, PIR, Matte, JJ and Zijlstra, RT 2010. In vitro starch digestion kinetics, corrected for estimated gastric emptying, predict portal glucose appearance in pigs. The Journal of Nutrition 140, 1227–1233.Google Scholar
Webb, KE, Matthews, JC and DiRienzo, DB 1992. Peptide absorption: a review of current concepts and future perspectives. Journal of Animal Science 70, 3248–3257.Google Scholar
Wilfart, A, Jaguelin-Peyraud, Y, Simmins, H, Noblet, J, Van Milgen, J and Montagne, L 2008. Kinetics of enzymatic digestion of feeds as estimated by a stepwise in vitro method. Animal Feed Science and Technology 141, 171–183.Google Scholar
Zayas, JF 1997. Functionality of proteins in food. Springer-Verlag, Berlin.Google Scholar