Proteolysis of meat and bone meal to increase utilisation
G. J. Piazza A B and R. A. Garcia AA US Department of Agriculture1, Agricultural Research Service, Eastern Regional Research Centre, Biobased and Other Animal Coproducts Research Unit, 600 East Mermaid Lane, Wyndmoor, PA 19038, USA.
B Corresponding author. Email: george.piazza@ars.usda.gov
Animal Production Science 54(2) 200-206 https://doi.org/10.1071/AN13041
Submitted: 1 February 2013 Accepted: 19 March 2013 Published: 7 May 2013
Abstract
Meat and bone meal (MBM), an important by-product of the meat industry, is the ground, rendered remainder of farm animals after removal of the hide and meat. Most protein in MBM is insoluble, which limits its usefulness. Defatted, milled porcine MBM was subjected to saturating amounts of trypsin, a selective protease, and subtilisin, a protease with broad selectivity. Samples were withdrawn over a 48-h time course of hydrolysis and filtered to remove insoluble material. The rate at which the MBM protein was converted to a soluble form was equivalent for both proteases. Over the time course, trypsin generated fewer free amino groups than did subtilisin, and at a specified time, the molecular weight (MW) of the soluble trypsin hydrolysate was higher than that of the subtilisin hydrolysate. Assay of amino group formation showed that the proteases were still active even after soluble protein generation had ceased. The hydrolysates are useful for a variety of food and non-food uses. The hydrolysates were tested for flocculation activity in an ongoing effort to find sources for renewable flocculant. Kaolin flocculant activity was observed with the soluble fraction obtained before hydrolysis of MBM and also observed with the relatively high MW hydrolysates from short treatment with trypsin and subtilisin. Low MW fractions obtained from by subtilisin treatment at 30–48 h also showed kaolin-settling ability, probably through a coagulation or charge neutralisation process.
Additional keywords: bridging, kaolin, patch.
References
Alvarez C, Rendueles M, Diaz 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 | 1:CAS:528:DC%2BC38XmvVKitrY%3D&md5=7a453b6ccfe69bb9520c64cbb204962dCAS |
Arvanitoyannis IS, Ladas D (2008) Meat waste treatment methods and potential uses. International Journal of Food Science & Technology 43, 543–559.
| Meat waste treatment methods and potential uses.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD1cXisFyktLg%3D&md5=a86e9066dbdef415f89002bf00f97b48CAS |
Bhaskar N, Modi VK, Govindaraju K, Radha C, Lalitha RG (2007) Utilization of meat industry by products: protein hydrolysate from sheep visceral mass. Bioresource Technology 98, 388–394.
| Utilization of meat industry by products: protein hydrolysate from sheep visceral mass.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD28XptlCqsL0%3D&md5=a409f5428890e023f08b978522583b29CAS | 16457999PubMed |
Bolto B, Gregory J (2007) Organic polyelectrolytes in water treatment. Water Research 41, 2301–2324.
| Organic polyelectrolytes in water treatment.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD2sXkvFWnur4%3D&md5=a5f2fff8b7de3ca05325d3494d866c66CAS | 17462699PubMed |
Bratby J (2006) ‘Coagulation and flocculation in water and wastewater treatment.’ 2nd edn. (IWA Publishing: London)
Bruckner P, Prockop DJ (1981) Proteolytic enzymes as probes for the triple-helical conformation of procollagen. Analytical Biochemistry 110, 360–368.
| Proteolytic enzymes as probes for the triple-helical conformation of procollagen.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaL3MXhtlGntbo%3D&md5=b5ac4676c648a5c974731836f3b49380CAS | 7015914PubMed |
Church FC, Porter DH, Catignani GL, Swaisgood HE (1985) An o-phthalaldehyde spectrophotometric assay for proteinases. Analytical Biochemistry 146, 343–348.
| An o-phthalaldehyde spectrophotometric assay for proteinases.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaL2MXhs1altL0%3D&md5=97e55534e7c678f604cc912a299257b9CAS | 3896021PubMed |
Garcia RA, Rosentrater KA, Flores RA (2006) Characteristics of North American meat and bone meal relevant to the development of non-feed applications. Applied Engineering in Agriculture 22, 729–736.
Garcia RA, Pyle DJ, Piazza GJ, Wen Z (2011) Hydrolysis of animal protein meals for improved utility in non-feed applications. Applied Engineering in Agriculture 27, 269–275.
Gehrke CW, Wall LL, Absheer JS (1985) Sample preparation for chromatography of amino acids: acid hydrolysis of proteins. Journal – Association of Official Analytical Chemists 68, 811–821.
Guérard F, Dufossé L, De La Broise D, Binet A (2001) Enzymatic hydrolysis of proteins from yellowfin tuna (Thunnus albacores) wastes using Alcalase. Journal of Molecular Catalysis. B, Enzymatic 11, 1051–1059.
| Enzymatic hydrolysis of proteins from yellowfin tuna (Thunnus albacores) wastes using Alcalase.Crossref | GoogleScholarGoogle Scholar |
Hill RL, Schmidt WR (1962) The complete enzymatic hydrolysis of proteins. The Journal of Biological Chemistry 237, 389–396.
Jayathilakan K, Sudtana K, Radhakrishna K, Bawa AS (2012) Utilization of byproducts and waste materials from neat, poultry and fish processing industries: a review. Journal of Food Science and Technology 49, 278–293.
| Utilization of byproducts and waste materials from neat, poultry and fish processing industries: a review.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BC38Xktlemu7w%3D&md5=0593a1f04f2e45cdd02d94af17e669a4CAS |
Lammens TM, Franssen MCR, Scott EL, Sanders JPM (2012) Availability of protein-derived amino acids as feedstock for the production of bio-based chemicals. Biomass and Bioenergy 44, 168–181.
| Availability of protein-derived amino acids as feedstock for the production of bio-based chemicals.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BC38Xptl2mtrg%3D&md5=8789f24c1489f37d7e5bb895f5db9e68CAS |
Liang Y, Garcia RA, Piazza GJ, Wen Z (2011) Nonfeed application of rendered animal proteins for microbial production of eicosapentaenoic acid by the fungus Pythium irregular. Journal of Agricultural and Food Chemistry 59, 11 990–11 996.
| Nonfeed application of rendered animal proteins for microbial production of eicosapentaenoic acid by the fungus Pythium irregular.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BC3MXhtlaqsLjK&md5=cc8c17dcf6b540cdb2d86b6b401ac022CAS |
Liu Y, Li K (2007) Development and characterization of adhesives from soy protein for bonding wood. International Journal of Adhesion and Adhesives 27, 59–67.
| Development and characterization of adhesives from soy protein for bonding wood.Crossref | GoogleScholarGoogle Scholar |
Nielsen PM, Petersen D, Dambmann C (2001) Improved method for determining food protein degree of hydrolysis. Food and Chemical Toxicology 66, 642–646.
Park SK, Bae DH, Hettiarachchy NS (2000) Protein concentrate and adhesives from meat and bone meal. Journal of the American Oil Chemists’. Society 77, 1223–1227.
Piazza GJ, Garcia RA (2010a) Meat and bone meal extract and gelatin as renewable flocculants. Bioresource Technology 101, 781–787.
| Meat and bone meal extract and gelatin as renewable flocculants.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD1MXht1amu7vO&md5=549b7e0d2880aca9f22fdc980732ef37CAS | 19734043PubMed |
Piazza GJ, Garcia RA (2010b) Proteins and peptides as renewable flocculants. Bioresource Technology 101, 5759–5766.
| Proteins and peptides as renewable flocculants.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BC3cXlt1SisLc%3D&md5=95c19bfb4b33316fb92822ede88a672eCAS | 20236820PubMed |
Rayner CJ (1985) Protein hydrolysis of animal feeds for amino acid content. Journal of Agricultural and Food Chemistry 33, 722–725.
| Protein hydrolysis of animal feeds for amino acid content.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaL2MXktlKhtrg%3D&md5=99f7c20fe1c76d7dfeb5ccbc2a86a28fCAS |
Salehizadeh H, Shojaosadati SA (2001) Extracellular biopolymeric flocculants, recent trends and biotechnological importance. Biotechnology Advances 19, 371–385.
| Extracellular biopolymeric flocculants, recent trends and biotechnological importance.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD3MXms1OksL8%3D&md5=d91913c83124d3179700e862c21e356eCAS | 14538073PubMed |
Solaiman DKY, Garcia RA, Ashby RD, Piazza GJ, Steinbüchel A (2011) Rendered-protein hydrolysates for microbial synthesis of cyanophycin biopolymer. New Biotechnology 28, 552–558.
| Rendered-protein hydrolysates for microbial synthesis of cyanophycin biopolymer.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BC3MXhtFymt7fI&md5=6857db8745d7f46678414ee75015ee9fCAS |
Sriperm N, Pesti GM, Tillman PB (2011) Evaluation of the fixed nitrogen-to-protein (N : P) conversion factor (6.25) versus ingredient specific N : P conversion factors in feedstuffs. Journal of the Science of Food and Agriculture 91, 1182–1186.
| Evaluation of the fixed nitrogen-to-protein (N : P) conversion factor (6.25) versus ingredient specific N : P conversion factors in feedstuffs.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BC3MXkt12hu7c%3D&md5=d2011be3540f2938d1bc54640787b7f0CAS | 21305546PubMed |
Swain SN, Biswal SM, Nanda PK, Nayak PJ (2004) Biodegradable soy-based plastics: opportunities and challenges. Journal of Polymers and the Environment 12, 35–42.
| Biodegradable soy-based plastics: opportunities and challenges.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD3sXovV2ks7w%3D&md5=8b007e2fa8cff1e2ffbb592128ff1315CAS |
Thomas AW, Seymour-Jones FL (1923) The hydrolysis of collagen by trypsin. Journal of the American Chemical Society 45, 1515–1522.
| The hydrolysis of collagen by trypsin.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaB3sXhsFyksQ%3D%3D&md5=605589780e375ddfe0e8077d3660a50aCAS |
Toldrá F, Aristoy M-C, Mora L, Reig M (2012) Innovations in value-addition of edible meat by-products. Meat Science 92, 290–296.
| Innovations in value-addition of edible meat by-products.Crossref | GoogleScholarGoogle Scholar | 22560456PubMed |
Vasileva-Tonkova E, Nustorova M, Gushterova A (2007) New protein hydrolysates from collagen wastes used as peptone for bacterial growth. Current Microbiology 54, 54–57.
| New protein hydrolysates from collagen wastes used as peptone for bacterial growth.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD28XhtlalurvF&md5=92444adead09d11de27f72cbb0c9005bCAS | 17171464PubMed |
Webster JD, Ledward DA, Lawrie RA (1982) Protein hydrolysates from meat industry by-products. Meat Science 7, 147–157.
| Protein hydrolysates from meat industry by-products.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaL3sXjs1On&md5=96393819e147f31e11f9ecf0e1170c82CAS | 22055137PubMed |
Yin S-W, Tang C-H, Cao J-S, Hu E-K, Wen Q-B, Yang X-B (2008) Effects of limited enzymatic hydrolysis with trypsin on the functional properties of hemp (Cannabis sativa L.) protein isolate. Food Chemistry 106, 1004–1013.
| Effects of limited enzymatic hydrolysis with trypsin on the functional properties of hemp (Cannabis sativa L.) protein isolate.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD2sXhtVerur7E&md5=464dfc03e952e79f0047cadc3e058347CAS |
Yuanlong C, Min C, Xiaoju C, Wenhua Z, Xuepin L, Bi S (2012) Enzymatic hydrolysis of skin shavings for preparation of collagen hydrolysates with specified molecular weight distribution. Journal of the Society of Leather Technologies and Chemists 96, 16–20.
Zhang G, Sun A, Li W, Liu T, Zhiguo S (2006) Mass spectrometric analysis of enzymatic digestion of denatured collagen for identification of collagen type. Journal of Chromatography. A 1114, 274–277.
| Mass spectrometric analysis of enzymatic digestion of denatured collagen for identification of collagen type.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD28XktVyis7Y%3D&md5=058fa52b9b4b76e9686646fd25def7abCAS | 16600269PubMed |