Influence of some commercial proteases and enzymatic associations on the hydrolytic solubilization of deboned poultry meat proteins Influencia de algunas proteasas comerciales y preparados enzimáticos en la solubilización hidrolitica de las proteínas de la carne de pollo separada mecánicamente

Abstract

Mechanically deboned poultry meat (MDPM) was used as a basic source of protein to assess the efficiency of seven proteolytic enzymes and some enzymatic associations over the hydrolysis of that protein. As a main parameter, the evolution of protein solubilization during 4 h of proteolysis was evaluated. The enzymes alcalase, esperase, flavourzyme, fungal protease, HT-proteolytic, papain, proteopex, and combinations of alcalase + flavourzyme, esperase + flavourzyme, HT-proteolytic + flavourzyme, and proteopex + flavourzyme were applied at concentrations of 0.60% and 1.20% of commercial product as a function of total protein. The initial pH was adjusted to 7.0 or 8.0 and the temperature was maintained at 50 °C or 60 °C according to optimal conditions for each enzyme. The proteolytic activities of the enzymes were also compared with azocasein. The hydrolysis index (HI), i.e., the rate between the maximum value and the initial amount of soluble protein was formulated to allow the comparison among treatments. Results showed that the temperature did not influence the proteolysis in the tested model. The association of alcalase + flavourzyme was shown to be more efficient than all other treatments, obtaining more than 70% of soluble protein. Fungal protease pre sented the lowest results.

Keywords

enzymes hydrolysis soluble proteins poultry meat

Get full access to this article

View all access options for this article.

References

Adler-Nissen J. (1976). Enzymatic hydrolysis of proteins for increased solubility. Journal of Agricultural and Food Chemistry 24 (6): 1090-1093.

Anderton A. , Howard J.P. and Scott D.W. (1986). Microbiological control of enteral feeding. Summary of a guidance document prepared on behalf of the Commitee of Parenteral and Enteral Nutrition Group of the British Dietetic Association. Human Nutrition, Applied Nutrition 40: 163-166.

Aoac (1990). Official Methods of Analysis of the Association of Official Analytical Chemists. Arlington, VA: Association of Official Analytical Chemists .

Cheftel J.C. , Cuq J.L. and Lorient D. (1989) Proteínas alimentarias: Bioquímica—Propriedades funcionales—Valor nutricional-Modificaciones químicas. Zaragoza, España: Acribia, 346 pp.

Cordle C.T. (1994). Control of Food Allergies Using Protein Hydrolysates . Food Technology 48 (10): 72-76.

Diniz F.M. and Martin A.M. (1998). Influence of process variables on the hydrolysis of shark muscle protein. Food Science and Technology International 4(2): 91-98.

Fik M. and Surówka K. (1986). Preparation and properties of protein concentrate from broiler chicken heads. Journal of the Science of Food and Agriculture 37: 445-453.

Freedland C.P. , Roller R.D. , Wolfe B.M. and Flynn N.M. (1989). Microbial contamination of continuous drip feeding . Journal of Parenteral and Enteral Nutrition 13: 18-21.

Freitas O. de , Padovan G.J. , Vilela L. , Santos J.E. dos , Oliveira J.E.D. and Greene L.J. (1993). Characterization of protein hydrolysates prepared for enteral nutrition. Journal of Agricultural and Food Chemistry 41 (1): 1432-1438.

10.

Kilara A. (1985). Enzyme-modified protein food ingredients. Process Biochemistry 20 (10): 49-157.

11.

Lahl W.J. and Braun S.D. (1994). Enzymatic production of protein hydrolysates for food use. Food Technology 48 (10): 68-71.

12.

Lin C.-W. and Su H.-P. (1986). Studies on the manufacture of a meat hydrolysate from spent hen for use as compound seasoning base. In: Fennema O.R. , Chang W.-H. and Lii C.-Y (eds), The Role of Chemistry in the Quality of Processed Foods. Westport, Connecticut : Food and Nutrition Press. pp.180-186.

13.

Ostovar K. , MacNeil J.H. and O'Donnell K. (1971). Poultry product quality. 5. Microbiological evaluation of mechanically deboned poultry meat. Journal of Food Science 36:1005-1007.

14.

Otte J. , Lomholt S.B. , Ipsen R. et al. (1997). Aggregate formation during hydrolysis of β-lactoglobulin with a Glu and Asp specific protease from Bacillus licheniformis. Journal of Agriculture and Food Chemistry 45: 4889-4896.

15.

Rebeca B.D. , Peña-Vera M.T. and Díaz-Castañeda M. (1991). Production of fish protein hydrolysates with bacterial proteases. Yield and nutritional value. Journal of Food Science 56 (2): 309-314.

16.

Sales A.M. , de Carvalho A.C.V. , Baldini V.L.S. , Gonçalves J.R. , Beraquet N.J. (1991). Extração enzímica de proteína de residuo de carne de frango mecanicamenta separada. Coletânea ITAL 21(2): 233-242.

17.

Sarath G. , de la Motte R.S. and Wagner F.W. (1989). Protease assay methods. In: Beynon R.J. and Bond J.S. (eds), Proteolytic Enzymes: A Practical Approach. Oxford, UK: IRL. pp. 25-55.

18.

Satterlee L.D. (1975). Improving utilization of animal by-products for human foods—a review. Journal of Animal Science 41 (2): 687-697.

19.

Scopes R.K. (1994). Protein Purification: Principles and Practice . 3rd edn. New York: Springer-Verlag.

20.

Sgarbieri V.C. (1996). Proteínas em alimentos protéicos: propriedades, degradações, modificações. São Paulo: Varela.

21.

Surówka K. and Fik M. (1992). Studies on the recovery of proteinaceous substances from chicken heads. I. An application of neutrase to the production of protein hydrolysate. International Journal of Food Science and Technology 27: 9-20.

22.

Surówka, K. and Fik M. (1994). Studies on the recovery of proteinaceous substances from chicken heads: II—Application of pepsin to the production of protein hydrolysate. Journal of the Science of Food and Agriculture 65: 289-296.

23.

Turgeon S.L. , Gauthier S.F. and Paquin P. (1992). Emulsifying property of whey peptide fractions as a function of pH and ionic strength. Journal of Food Science 57 (3): 601-604.

24.

Webster J.D. , Ledward D.A. and Lawrie R.A. (1982). Protein hydrolysates from meat industry by-products. Meat Science 7: 147-157.