Czech J. Food Sci., 2002, 20(1):1-6 | DOI: 10.17221/3502-CJFS

Effect of temperature and enzyme/substrate ratio on the hydrolysis of pea protein isolates by trypsin

M. Karamaĉ, R. Amarowicz, H. Kostyra
Institute of Animal Reproduction and Food Research of Polish Academy of Sciences - Division of Food Science, Olsztyn, Poland

Two pea protein isolates, Pisane and Propulse, were hydrolysed by trypsin. The degree of hydrolysis (DH) was computed using a pH-stat method. Enzymatic treatment of the pea protein isolates was conducted at four different temperatures, namely 35, 40, 45 and 50°C. The relationship between DH and E/S ratio was studied at 50°C and at four different E/S ratios; these were 5, 15, 25, 35 mAU/g (AU - Anson unit). For Pisane the highest value of the final DH (10.4%) was obtained at 45°C, whereas for Propulse the optimal temperature was 50°C and a DH value of 13.2% was attained. In the case of Pisane, the highest DH (11.5%) was recorded if the enzyme/substrate ratio was 35 mAU/g whereas for Propulse, the highest DH (13.2%) was observed at an E/S ratio of 15 mAU / g.

Keywords: pea; protein isolates; enzymatic hydrolysis; enzyme, substrate ratio; temperature; trypsin

Published: February 28, 2002  Show citation

ACS AIP APA ASA Harvard Chicago Chicago Notes IEEE ISO690 MLA NLM Turabian Vancouver
Karamaĉ M, Amarowicz R, Kostyra H. Effect of temperature and enzyme/substrate ratio on the hydrolysis of pea protein isolates by trypsin. Czech J. Food Sci. 2002;20(1):1-6. doi: 10.17221/3502-CJFS.
Download citation

References

  1. ADLER-NISSEN J. (1984): Control of proteolytic reaction and the level of bitterness in protein hydrolysis processes. J. Chem. Tech. Biotechnol., 34B: 215-222. Go to original source...
  2. ADLER-NISSEN J. (1986): Enzymatic hydrolysis of food proteins. Elsevier, London: 132-142.
  3. ADSULE R.N., LAWANDE K.M., KADAM S.S. (1989): Pea. In: SALUNKHE D.K., KADAM S.S. (eds): CRC Handbook of World Food Legumes: Nutritional, Chemistry, Processing, Technology, and Utilization. Vol. II. CRC Press Inc., Boca Raton: 215-251.
  4. AMAROWICZ R., SHAHIDI F. (1997): Antioxidant activity of peptide fractions of capelin protein hydrolysates. Food Chem., 58: 355-359. Go to original source...
  5. BHATTY R.S. (1988): In vitro hydrolysis of pea, faba bean and lentil meals and isolated protein fractions by pepsin and trypsin. Can. Inst. Food Sci. Technol. J., 21: 66-71. Go to original source...
  6. BOMBARA N., PILSOF M.R., AÑON M.C. (1992): Kinetics of wheat proteins solubilization with a fungal protease. Lebens. Wiss. Technol., 25: 527-531.
  7. CONSTANTINIDES A., ADU-AMANKWA B. (1980): Enzymatic modification of vegetable protein: mechanism, kinetics, and production of soluble an partially soluble protein in a batch reactor. Biotechnol. Bioeng., 22: 1543-1565. Go to original source...
  8. GONZÁLEZ-TELLO P., CAMACHO F., JURADO E., PÁEZ M.P., GUADIX E.M. (1994): Enzymatic hydrolysis of whey proteins: I. Kinetic model. Biotechechnol. Bioeng., 44: 523- 528. Go to original source... Go to PubMed...
  9. GWIAZDA S., RUTKOWSKI A., KOCOÑ J. (1979): Some functional properties of pea and soybean protein preparations. Nahrung, 23: 681-686. Go to original source...
  10. GWIAZDA S., WYRZYKOWSKA A., WASYLUK K. (1994): Comparison of selected method for determination the degree of hydrolysis of rapeseed proteins. Pol. J. Food Nutr. Sci., 3/44: 165-173.
  11. HORVATH E., ORMAI-CSERHALMI Z., CZUKOR B. (1989): Functional properties of air classified yellow peas (Pisum sativum) fractions. J. Sci. Food Agr., 49: 493-497. Go to original source...
  12. FROKJAER S. (1994): Use of hydrolysates for protein supplementation. Food Technol., 98, No 9: 86-88.
  13. HAJÓS G., ÉLIÁS I., HALÁSH A. (1988). Methionine enrichment of milk protein by enzymatic peptide modification. J. Food Sci., 53: 739-742. Go to original source...
  14. KARAMAĈ M., AMAROWICZ R., KOSTYRA H., SIJTSMA L. (1998). Hydrolysis of pea protein isolate Pisane by trypsin. Nahrung, 42: 219. Go to original source...
  15. MAHMOUD M.L, MALONE W.T., CORDLE C.T. (1992): Enzymatic hydrolysis of casein: Effect of degree of hydrolysis on antigenicity and physical properties. J. Food Sci., 57: 1223-1229. Go to original source...
  16. MARGOT A., FLASCHEL E., RENKE A. (1997): Empirical kinetic models for tryptic whey-protein hydrolysis. Process Biochem., 32: 217-223. Go to original source...
  17. O'MEARE G.M., MUNRO P.A. (1985): Kinetics of the hydrolysis of lean meat protein by Alcalase: Derivation of two alternative rate equations and their fit to experimental data. Biotechnol. Bioeng., 27: 861-869. Go to original source... Go to PubMed...
  18. PANASIUK R., AMAROWICZ R., KOSTYRA H., SIJTSMA L. (1998): Determination of α-amino nitrogen in pea protein hydrolysates: a comparison of three analytical methods. Food Chem., 62: 363-367. Go to original source...
  19. P AREDES-LOPEZ O., ORDORICA-FALOMIR C., OLIVARESVAZQUEZ M.R. (1991): Chickpea protein isolates: physicochemical, functional and nutritional characterization. J. Food Sci., 56: 726-729. Go to original source...
  20. POULIOT Y., GAUTHIER S.F., BARD C. (1995): Skim milk solids as substrate for the preparation of casein enzymatic hydrolysates. J. Food Sci., 60: 111-116. Go to original source...
  21. SHAHIDI F., AMAROWICZ R. (1996): Antioxidant activity of protein hydrolyzates from aquatic species. J. Am. Oil Chem. Soc., 73: 1197-1199. Go to original source...
  22. SCHMIDL M.K., TAYLOR S.L., NORDLEE J.A. (1994): Use of hydrolysate-based products in special medical diets. Food Technol., 48: 77-85.
  23. SHIH F.F. (1990): Deamidation during treatment of soy protein with protease. J. Food Sci., 55: 127-132. Go to original source...
  24. SIJTSMA L., TEZERA D., HUSTINX J., VEREIJKEN J.M. (1998): Improvement of pea protein quality by enzymatic modification. Nahrung, 42: 215 -216. Go to original source...
  25. SORAL-ĤMIETANA M., SWIGOÑ A., AMAROWICZ R., SIJTSMA L. (1998): The solubility of trypsin pea protein hydrolysates. Nahrung, 42: 217-218. Go to original source...
  26. VAINTRAUB I.A., BASSÜNER R., SHUTOV A.D. (1976): The action of trypsin and chymotrypsin on the reserve proteins of some leguminous seeds. Nahrung, 20: 763-771. Go to original source... Go to PubMed...

This is an open access article distributed under the terms of the Creative Commons Attribution-NonCommercial 4.0 International (CC BY NC 4.0), which permits non-comercial use, distribution, and reproduction in any medium, provided the original publication is properly cited. No use, distribution or reproduction is permitted which does not comply with these terms.