Register      Login
Animal Production Science Animal Production Science Society
Food, fibre and pharmaceuticals from animals
RESEARCH ARTICLE

Alkaline hydrolysis of porcine blood haemoglobin: applications for peptide and amino acid production

Carlos Álvarez A , Manuel Rendueles A and Mario Díaz 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 53(2) 121-128 https://doi.org/10.1071/AN12148
Submitted: 16 February 2012  Accepted: 18 July 2012   Published: 30 October 2012

Abstract

Alkaline hydrolysis of proteins recovered from slaughterhouse blood is a method to obtain profitable peptides and free amino acids for animal feed, besides decreasing the waste produced by this industry. The current trend to use enzymatic hydrolysis may need reconsidering due to its high cost in materials and the need for control processes that are both complex and expensive. The use of caustic soda (NaOH), which is a low-cost product, to obtain useful peptides from porcine haemoglobin is studied in this paper. Concentrations of 6 M NaOH at 50°C for 24 h afforded an 80% peptide recovery yield with an average peptide size of 13 kDa. Product obtained at 24 h was composed of soluble haemoglobin (7%), peptides larger than 10 kDa (63%), peptides between 6 and 10 kDa (16%), peptides between 1 and 6 kDa (1%), free amino acids (4%) and non-soluble compounds (8%). A kinetic model was subsequently developed. It is proposed that neutralising the alkaline product using acid products allows the processing of a higher amount of protein while employing the same amounts of reagents, although this topic requires further research.


References

Álvarez C, Bances M, Rendueles M, Díaz M (2009) Functional properties of isolated porcine blood proteins. International Journal of Food Science & Technology 44, 807–814.
Functional properties of isolated porcine blood proteins.Crossref | GoogleScholarGoogle Scholar |

Álvarez C, Rendueles M, Díaz M (2012) The yield of peptides and amino acids following acid hydrolysis of haemoglobin from porcine blood. Animal Production Science 52, 313–320.
The yield of peptides and amino acids following acid hydrolysis of haemoglobin from porcine blood.Crossref | GoogleScholarGoogle Scholar |

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 number 2 657 232.

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 and Agriculture 30, 809–815.

Flork M (1989) Industrial process for the preparation of amino acids by hydrolysis of proteins in acid medium. Unites States Patent number 4 874 893.

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 |

Grimble GK, Rees RG, Keohane PP, Cartwright T, Desreumaux M, Silk DB (1987) Effect of peptide chain length on absorption of egg protein hydrolysates in the normal human jejunum. Gastreoenterology 92, 136–142.

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 |

Luo J, Ding L, Chen X, Wan Y (2009) Desalination of soy sauce by nanofiltration. Separation and Purification Technology 66, 429–437.

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 |

Ockerman HW, Hansen CL (1994) ‘Industrialización de Subproductos de Origen Animal.’ (Acribia: Zaragoza, Spain)

Ozols J (1990) ‘Methods in enzymology. Vol. 182.’ (Academic Press: San Diego)

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 haemoglobin. European Food Research and Technology 225, 637–647.
Time-dependent nature peptic hydrolysis of native bovine haemoglobin.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 haemoglobin 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 haemoglobin 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 |

Yu Y, Hu J, Bai X, Du Y, Lin B (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 | 1:CAS:528:DC%2BD28XltVKnsrw%3D&md5=a51f436da75603a52ec2c494252f0abbCAS |