Proceedings book download - 5Z.com

We studied molecular-weight distribution of CMPC hydrolyzates which were derivedusing such enzymatic agents as ''Flavourzyme'', ''Pancreatin'' and EARKCH. Theirconcentrations varied from 0.5% to 5.0%. It was found that in the hydrolyzate obtainedwith 5.0 % Flavourzyme concentration the percentage of high-molecular structures halved,whereas the fraction of short-chain peptides and free amino acids increased by 1,7 timescompared to the relevant indices for the hydrolyzate derived with 0.5% Flavourzymeconcentration.Cow milk protein concentrate was fermented by ''Pancreatin'' with two concentrations(0.5% and 2.0%) and stable 7.5 pH for 8 hours. With 0.5% concentration and optimal pHthe fraction of high-molecular structures in hydrolyzate did not exceed 6% and the lowmolecularfraction reached nearly 60%. Similar values were recorded for hydrolyzatederived by proteolysis of CMPC with 2% ''Flavourzyme''.Thus, the lowest content of high-molecular structures in obtained products is recordedfor hydrolysis with ''Pancreatin'' and stable pH for 8 hours when concentration of all thetested enzymatic agents is 0.5%. However, ''foreign'' macroelements, such as sodium orpotassium, occurred at optimal pH are undesirable to further application of enzymolyzate asa complex with EM [6,7].With low concentration (0.5%) EARKCH is more efficient than ''Flavourzyme''. Whenenzyme-to-substrate ratio increases the efficiency of proteolysis with these enzymaticagents is similar if to estimate it by molecular-weight distribution of peptide fractions ofderived hydrolyzates.High content of peptides with molecular weight under 1.4 kD in essentialmicroelement complexes with enzymolyzate of cow milk proteins is unwanted for somereasons.First of all, abundant low-molecular fractions in the complex increase osmomolarity ofthe obtained agent which is extremely undesirable to its further application for foodfortification [7,8].Secondly, these fractions make products bitter which will have a significant influenceon their application in food industry [9,10].Thirdly, we demonstrated earlier that cow milk protein structures with molecularweight under 1 kD and above 10 kD are less efficient in microelement binding [4,11,12].The latter is probably dependent on the features of steric structure of peptide molecules.It should be mentioned that EARKCH utilization is more efficient in respect totechnology and microbiological control since this enzyme is active at low temperatureswhich considerably delay the development of microflora including pathogenic one.Thus, formation of EM complexes containing peptides with molecular weight from1.4 kD to 11.2 kD derived by proteolysis using the enzymatic agent from the red king crabhepatopancreas is considered to be the most optimal and efficient.References1. Mukhin, V.A., Novikov, V.Yu. 2001. Enzymatic protein hydrolyzate of tissues of marinehydrobionts: obtainment, characteristics and practical use. PINRO Press, Murmansk. 97 pp. (inRussian).2. Mukhin, V.A., Novikov, V.Yu., Ryzhikova, L.S. Appl. Biochem. Microbiol. 37 (3), 292-296 (2001).3. Vegarud, G.E., Langsrud, T., Svenning, C. British J. Nutr. 84 (1), 91-98 (2000).4. Swain, J.H., Tabatabai, L.B., Reddy, M.B. The J. Nutr. 132 (2), 245-251 (2002).5. Mukhin, V.A., Novikov, V.Yu. Proteolysis and proteolytic enzymes in the tissues of marineinvertebrates. PINRO Press, Murmansk, 2002 (in Russian).6. Manual for methods of analysis of food product quality and safety. Ed. by I. M. Skurikhin andTutelyan. Brandes-medicine Press, Moscow. P. 183-185 (in Russian).7. Popova, T.S., Tamazashvily, T.Sh., Shestopalov, A.E. Parenteral and enteral nutrition in surgery.''M-CITY'' Press, Moscow, 1996 (in Russian).8. Neklyudov, A.D., Ivankin, A.N., Berdutina, A.V. Appl. Biochem. Microbiol. 36 (5), 452-459 (2000).9. Mahmoud, M.I. Food Technol. 48 (10), 89-95 (1994).10. Pedersen, P. Food Technol. 48 (10), 96-98 (1994).11. Etcheverry, P., Miller, D.D., Glahn, R.P. The J. Nutr. 134 (1), 93-98 (2004).12. Serfass, R.E., Reddy, M.B. The J. Nutr. 133 (2), 449-455 (2003).541