• M.E. Rodríguez-Huezo Tecnológico de Estudios Superiores de Ecatepec
  • D.L. Villagómez-Zavala Facultad de Estudios Superiores Cuautitlán. Universidad Nacional Autónoma de México
  • B. Lozano-Valdés Universidad Iberoamericana
  • R. Pedroza-Islas Universidad Iberoamericana
Keywords: protein hydrolysates, hydrolysis degree, emulsifying activity, foaming activity, fat retention capability


The surface properties of commercial protein hydrolysates from fish (FPH), bovine serum (BSPH), maize by acid hydrolysis (MPHA) and maize by enzymatic hydrolysis (MPHE) were evaluated. The emulsifying activity (EA), stability (ES), and capacity (EC); foaming capacity (FC) and stability (FS); fat holding capacity (FHC); and solubility (S) were determined. Electric conductivity was used for evaluating the emulsifying properties. Average molecular weights were determined by SDS-PAGE. FC was determined by measuring the percentage increase in volume of the hydrolysates solutions upon stirring, whilst FS was determined by measuring the remaining foam volume after a given period of time. MPHA displayed the best EA (255 µS) (p < 0.05); MPHE showed the best ES (49.14 min) (p < 0.05); MPHA and MPHE exhibited the highest FHC values (6.7 mL/g); and MPHE had the highest FC (62.5%) (p < 0.05). FPH displayed the highest EC (340 g oil/g protein) (p < 0.05). Highest FS was shown by MPHA. In general, the best overall properties were displayed by the maize hydrolysates.


Adler-Nissen, J. (1986). Enzymatic hydrolysis of food proteins. Elsevier Applied Science Publishers, London, UK.

AOAC, (2000). “Official Methods of Analysis” 17T h ed., Association of Official Analytical Chemists, Washington, DC.

Caessens, P., Visser, S., Gruppen, H., and Voragen, A.G.J. (1999). β-lactoglobulin hydrolysis. I. Peptide composition and functional properties of hydrolysates obtained by the action of plasmin, trypsin, and Staphilococcus aureus V8 protease. Journal of Agricultural and Food Chemistry 47, 2973-2979.

Chabanon, G., Chevalot, I., Framboisier, X., Chenu, S. and Marc, I. (2007). Hydrolysis of rapeseed protein isolates: Kinetics, characterization and functional properties of hydrolysates. Process Biochemistry 42, 1419-1428.

Cheftel, J.C., Cuq, J.L. and Lorient, D. (1989). Proteínas alimentarias, Pp. 115- 120. Editorial Acribia, España.

Dickinson, E. (2001). Milk protein interfacial layers and the relationship to emulsion stability and rheology. Colloid & Surfaces B 20, 197-210.

Dickinson, E. and McClements, J. (1996). Advances in food colloids. Blackie Academic & Professional. London.

Forstrom, C. K., Vegarud, G., Langsrud, T., Risberg, E. M., and Egelandsdal, B. (2004). Hydrolyzed whey proteins as emulsifiers and stabilizers in high-pressure processed dressing. Food Hydrocolloids 18, 757-767.

Garti, N., Magdasi, S., and Rubinstein, A. (1981). A new method for stability determination of semi-solid emulsions, using conductivity measurements. Colloids & Surfaces 3 (3), 221-231.

Gornall, A.G., Bardawill, C.J., and David, M.M. (1949). Determining serum proteins by means of the biuret reaction. Journal of Biological Chemistry 177, 751-766.

Jamdar, S.N., Rajalakshmi, V., Pednekar, M.D., Juan, F., Yardi, V., and Sharma, A. (2010). Influence of degree of hydrolysis on functional properties, antioxidant activity and ACE inhibitory activity of peanut protein hydrolysate. Food Chemistry 121, 178-184.

Hordur, G., Kristinson, B. and Rasco, A. (2000). Fish protein hydrolysates: Production, biochemical, and functional properties. Critical Reviews in Food Science and Nutrition 40 (1), 43-81.

Kato, A., Fujishige, T., Matsudommi, N. and Kobayashi, K. (1985). Determination of emulsifying properties of some proteins by conductivity measurements. Journal of Food Science 50, 56-59.

Kelfala, M.B., Amadou, I., Foh, B.M., Kamara, M.T., and Xia, W. (2010). Functionality and antioxidant properties of tilapia (Oreochromis niloticus) as influenced by the degree of hydrolysis. International Journal of Molecular Science 11, 1851-1869.

Kristinsson, H., and Rasco, B. (2000). Biochemical and functional properties of Atlantic salmon (Salmo salar) muscle proteins hydrolyzed with various alkaline proteases. Journal of Agricultural and Food Chemistry 48, 657-666.

Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685

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

Liceaga-Gesualdo, A.M. and Li-Chan, E.C.Y. (1999). Functional properties of fish protein hydrolysate from herring (Clupea harengus). Journal of Food Science 64, 1000-1004.

Linder, M., Fanni, J., and Parmentier, M. (1996). Functional properties of veal bone hydrolysates. Journal of Food Science 61, 712-720.

Liu, Q., Kong, B., Xiong, Y.L., and Xia, X. (2010). Antioxidant activity and functional of porcine plasma protein hydrolysate as influenced by the degree of hydrolysis. Food Chemistry 118, 403-410.

Mahmoud, M.I. (1994). Physicochemical and functional properties of protein hydrolysates in nutritional products. Food Technology 48(10), 89-94.

Mahmoud, M.I., and Cordle, C.T. (2000). Protein hydrolysates as special nutritional ingredients. In: Novel macromolecules in food systems (G. Doxastakis and V. Kiosseoglou, eds.), Pp. 181-215. Elsevier, Amsterdam.

Martínez, K.D., Carrera, S.C., Rodríguez-Patiño, J.M. and Pilosof, A.M.R. (2009). Interfacial and foaming properties of soy protein and their hydrolysates. Food Hydrocolloids 23, 2149-2157.

McClements, D.J. (1999). Food emulsions: Principles, practice, and techniques. CRC Press, Boca Raton, FL.

Miñones, C.J., and Rodríguez-Patiño, J.M. (2007). Phospholipids and hydrolysates from a sunflower protein isolate adsorbed at the air-water interface. Food Hydrocolloids 21, 212-220.

Mitchell, J.R., and Ledward, D.A. (1986). Functional properties of food macromolecules. Elsevier Applied Science Publishers. London.

Morr, C.V., German, B., Kinsella, J. E., Regenstein, J.M., Van Buren, J.P., Kilara, A., Lewis, B.A, and Mangino, M.E. (1985). A collaborative study to develop a standardized food protein solubility procedure. Journal of Food Science 50, 1715-1718.

Ninsang, S., Lertsiri, S., Suphantharika, M., and Assavanig, A. (2005). Optimization of enzymatic hydrolysis of fish soluble concentrate by commercial proteases. Journal of Food Engineering 70, 571-578.

Pacheco-Aguilar, R., Mazorra-Manzano, M.A., and Ramírez-Suárez, J.C. (2008). Functional properties of fish protein hydrolysates from Pacific whiting (Merluccius products) muscle produced by a commercial protease. Food Chemistry 109, 782-789.

PDFTop (2010). Emulsions.http://www.pdftop. com/ebook/emulsions/ intephen01/ files/06 emulsion.ppt. Accessed August 4, 2010.

Pedersen, B. (1994). Removing bitterness from protein hydrolysates. Food Technology 48(10), 96-99.

Pedroche, J., Yust, M.M., Lqari, H., Girón-Calle, J., Alaniz, M., and Vioque J. (2004). Brassica carinata protein isolates: Chemical composition protein characterization and improvement of functional properties by protein hydrolysis. Food Chemistry 88, 337- 346.

Petruccelli, S.,and Añón, M.C. (1994). Relationship between the method of obtention and structural and functional properties of soy protein isolates. 1. Structural and hydration properties. Journal of Agricultural and Food Chemistry 42, 2161-2169.

Swift, C. E., and Sulzbzcher, W. L. (1963). Factors affecting meat proteins as emulsion stabilizers. Food Technology 15, 224-226.

Walstra, P. (2003). Physical chemistry of foods. Marcel Dekker, Inc. New York.

Wilde, P. (2000). Interfaces: Their role in foam and emulsion behavior. Current Opinion in Colloid and Interface Science 5, 176-181.
How to Cite
Rodríguez-Huezo, M., Villagómez-Zavala, D., Lozano-Valdés, B., & Pedroza-Islas, R. (2020). SURFACE PROPERTIES OF MAIZE, FISH AND BOVINE SERUM PROTEIN HYDROLYSATES. Revista Mexicana De Ingeniería Química, 9(3), 241-250. Retrieved from

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