The yield of peptides and amino acids following acid hydrolysis of haemoglobin from porcine blood
Carlos Alvarez A , Manuel Rendueles A and Mario Diaz A B
+ Author Affiliations
- Author Affiliations
A Department of Chemical Engineering and Environmental Technology, University of Oviedo, Oviedo, Spain.
B Corresponding author. Email: mariodiaz@uniovi.es
Animal Production Science 52(5) 313-320 https://doi.org/10.1071/AN11218
Submitted: 7 October 2011 Accepted: 18 January 2012 Published: 10 May 2012
Abstract
Animal blood is the most important waste product from the meat industry due to the huge volumes produced and its pollutant power. Different methods are currently employed to process this by-product, such as drying, incineration or enzymatic hydrolysis. All these techniques are expensive, do not result in revalorisation or are not applicable at an industrial scale. In this paper, chemical hydrolysis is presented as an alternative to recover and increase the value of purified haemoglobin, the most abundant protein in blood. Non-enzymatic hydrolysis of haemoglobin is a good method for obtaining peptides due to its low cost, ease of control and the large amount of peptides produced, as well as being suitable for industrial applications. This paper presents a study of the use of two acids (sulfuric and hydrochloric) for this purpose under different experimental conditions. From the analysis of the kinetics of the hydrolysis process, four fractions can be defined: unbroken haemoglobin, soluble peptides, non-soluble peptides and free amino acids. A kinetic model was developed to simulate the hydrolysis mechanisms, providing a good fit to the experimental results. Both sulfuric and hydrochloric acid at concentrations of 6 M can hydrolyse the haemoglobin completely, but the average peptide size is lower for sulfuric than for hydrochloric acid.
Additional keywords: animal feed, peptide size, wastes.
References
Bautista J, Corpas R, Cremades O, Hernandez-Pinzon I, Romos R, Villaneuva A (2000) Sunflower protein hydrolysates for dietary treatment of patients with liver failure. Journal of the American Oil Chemists’ Society 77, 121–126.| Sunflower protein hydrolysates for dietary treatment of patients with liver failure.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD3cXhsVOnsrY%3D&md5=82c416b4a6deac8009539d575d91539dCAS |
Borkenhagen LK (1953) Process for preparing amino acids. United States Patent No. 2657232.
Clemente A (2000) Enzymatic protein hydrolysates in human nutrition. Trends in Food Science & Technology 11, 254–262.
| Enzymatic protein hydrolysates in human nutrition.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD3MXit1Wgu7g%3D&md5=5db457b786e0a8b6c6560883edb52f62CAS |
de Vouno M, Penteado C, Lajolo Franco M, Pereira Dos Santos N (1975) Functional and nutritional properties of isolated bovine blood proteins. Journal of the Science of Food and Agriculture 30, 809–815.
Flork M (1989) Industrial process for the preparation of amino acids by hydrolysis of proteins in acid medium. United States Patent No. 4874893.
Fountoulakis M, Hans-Werner L (1998) Hydrolysis and amino acid composition analysis of proteins. Journal of Chromatography. A 826, 109–134.
| Hydrolysis and amino acid composition analysis of proteins.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaK1MXjsFah&md5=98db959daf381bb2816f0101adb7c35eCAS |
Gauthier SF, Vachon C, Savoie L (1986) Enzymatic conditions of an in vitro method to study protein digestion. Journal of Food Science 51, 960–964.
| Enzymatic conditions of an in vitro method to study protein digestion.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaL28XlslSqsL4%3D&md5=6d1979a9fef2a71481510b8cee650798CAS |
Liu XQ, Yonekura M, Tsutsumi M, Sano Y (1996) Physicochemical properties of aggregates of globin hydrolysates. Journal of Agricultural and Food Chemistry 44, 2957–2961.
| Physicochemical properties of aggregates of globin hydrolysates.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaK28XlvVertLk%3D&md5=ea5bf3b5e7ef3f5cc848dcfb313db44bCAS |
Liu TX, Wang J, Zhao MM (2010) In vitro haem solubility of red cell fraction of porcine blood under various treatments. International Journal of Food Science & Technology 45, 719–725.
| In vitro haem solubility of red cell fraction of porcine blood under various treatments.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BC3cXltVCktbc%3D&md5=83e71054e912cf5adf71ee3d708bef07CAS |
Noordman TR, Ketelaar TH, Donkers F, Wesselingh JA (2002) Concentration and desalination of protein solutions by ultrafiltration Chemical Engineering Science 57, 693–703.
| Concentration and desalination of protein solutions by ultrafiltrationCrossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD38XhtVSmu7c%3D&md5=223ebb563f9a93f63f14617b70ebc6f6CAS |
Ozols J (1990) ‘Methods in enzymology. Vol. 182.’ (Ed. MP Deutscher) (Academic Press: San Diego, CA)
Ravindran G, Bryden WL (2005) Tryptophan determination in proteins and feedstuffs by ion exchange chromatography. Food Chemistry 89, 309–314.
| Tryptophan determination in proteins and feedstuffs by ion exchange chromatography.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD2cXms1CmtL4%3D&md5=8038095ff668baa9616c4d461e278113CAS |
Rendueles M, Moure F, Fernández A, Díaz M (1997) Preliminary studies on the processing of slaughter-house blood for protein recovery. Resource and Environmental Biotechnology 1, 193–206.
Rogalinski T, Herrmann S, Brunner G (2005) Production of amino acids from bovine serum albumin by continuous sub-critical water hydrolysis. The Journal of Supercritical Fluids 36, 49–58.
| Production of amino acids from bovine serum albumin by continuous sub-critical water hydrolysis.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD2MXhtVSqs7%2FM&md5=1b692bc0e29c21ec2632948c751981b2CAS |
Rosen H (1957) A modified ninhydrin colorimetric analysis for amino acids. Archives of Biochemistry and Biophysics 67, 10–15.
| A modified ninhydrin colorimetric analysis for amino acids.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaG2sXks1ersA%3D%3D&md5=c9b9e3da6cd1d2567aad7371ac3588f8CAS |
Su RX, Qi W, He ZM (2007) Time-dependent nature peptic hydrolysis of native bovine hemoglobin. European Food Research and Technology 225, 637–647.
| Time-dependent nature peptic hydrolysis of native bovine hemoglobin.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD2sXosVSmsr0%3D&md5=d0c98991904ea2dc59b9a52fe192ba58CAS |
Tauzin J, Miclo L, Roth S, Mollé D, Gaillard JL (2003) Tryptic hydrolysis of bovine αS2-casein: identification and release kinetics of peptides. International Dairy Journal 13, 15–27.
| Tryptic hydrolysis of bovine αS2-casein: identification and release kinetics of peptides.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD3sXht1GitbY%3D&md5=e607226362848e63dfe6380f6cc07c2fCAS |
Vaghefi N, Nedjaoum F, Guilochon D, Bureau F, Arhan P, Bouglé D (2002) Influence of the extent of hemoglobin hydrolysis on the digestive absorption of heme iron. An in vitro study. Journal of Agricultural and Food Chemistry 50, 4969–4973.
| Influence of the extent of hemoglobin hydrolysis on the digestive absorption of heme iron. An in vitro study.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD38XlsVCgs7Y%3D&md5=0a0c59348edf518bf0cd4d326eb80883CAS |
Vanhoute M, Firdaous L, Bazinet L, Froidevaux R, Lecouturier D, Guillochon D, Dhulster P (2010) Effect of haem on the fractionation of bovine haemoglobin peptic hydrolysate by electrodialysis with ultrafiltration membranes Journal of Membrane Science 365, 16–24.
| Effect of haem on the fractionation of bovine haemoglobin peptic hydrolysate by electrodialysis with ultrafiltration membranesCrossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BC3cXhtlKmsbjM&md5=5185ef17112c6fd42d5eec4e51ab0809CAS |
Vijayalakshmi MA, Lemieux L, Amoit J (1986) High performance size exclusion liquid chromatography of small molecular weight peptides from protein hydrolysates using methanol as a mobile phase additive. Journal of Liquid Chromatography 9, 3559–3576.
| High performance size exclusion liquid chromatography of small molecular weight peptides from protein hydrolysates using methanol as a mobile phase additive.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaL2sXpvVOrsQ%3D%3D&md5=68573c88fdf408623069f1fe992d9227CAS |
Williams PEV (1995) Digestible amino acids for non-ruminant animals: theory and recent challenges. Animal Feed Science and Technology 53, 173–187.
| Digestible amino acids for non-ruminant animals: theory and recent challenges.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaK2MXntFSjs74%3D&md5=6b8569eca7ee1bc0997760e85f28433dCAS |
Yike Y, Jianen H, Xuefeng B, Yuguang D, Bingcheng L (2006) Preparation and function of oligopeptide-enriched hydrolysate from globin by pepsin. Process Biochemistry 41, 1589–1593.
| Preparation and function of oligopeptide-enriched hydrolysate from globin by pepsin.Crossref | GoogleScholarGoogle Scholar |
