Improving the colloidal and sensory properties of a caseinate hydrolysate using particular exopeptidases.
作者： Jacob Ewert , Felix Schlierenkamp , Lena Nesensohn , Lutz Fischer , Timo Stressler
DOI: 10.1039/C8FO01749B
关键词:
摘要: Enzymatic hydrolysis with endopeptidases can be used to modify the colloidal properties of food proteins. In this study, sodium caseinate was hydrolyzed Sternzym BP 25201, containing a thermolysin-like endopeptidase from Geobacillus stearothermophilus as only peptidase, DH 2.3 ± 1%. The hydrolysate (pre-hydrolysate) obtained increased in its foam (+35%) and emulsion stability (+200%) compared untreated but showed bitter taste. This further treated exopeptidases PepN, PepX or PepA, acting on N-terminus peptides. Depending specificity exopeptidase used, changes regarding (hydrophobicity, size), behavior (emulsions, foams) taste were observed. No bitterness improvements (foam: +69%, emulsion: +29%) determined after application which is specific for hydrophilic amino acids Asp, Glu Ser. By contrast, treatment general aminopeptidase PepN resulted non-bitter product, no significant pre-hydrolysate (p < 0.05). Similar results those (reduced pre-hydrolysate, enhanced caseinate) also using commercial Flavourzyme, reduced activity (exo-flavourzyme). conclusion, modifications applied offer potent tool researchers industry produce protein hydrolysates properties.
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sci-hub.se 参考文章(43)
Michael Merz, Jacob Ewert, Claudia Baur, Daniel Appel, Imre Blank, Timo Stressler, Lutz Fischer, Wheat gluten hydrolysis using isolated Flavourzyme peptidases: Product inhibition and determination of synergistic effects using response surface methodology Journal of Molecular Catalysis B-enzymatic. ,vol. 122, pp. 218- 226 ,(2015) , 10.1016/J.MOLCATB.2015.09.010
R.J. FitzGerald, G. O'Cuinn, Enzymatic debittering of food protein hydrolysates Biotechnology Advances. ,vol. 24, pp. 234- 237 ,(2006) , 10.1016/J.BIOTECHADV.2005.11.002
Timo Stressler, Thomas Eisele, Bertolt Kranz, Lutz Fischer, PepX from Lactobacillus helveticus: Automated multi-step purification and determination of kinetic parameters with original tripeptide substrates Journal of Molecular Catalysis B-enzymatic. ,vol. 108, pp. 103- 110 ,(2014) , 10.1016/J.MOLCATB.2014.07.006
Michael T. McCaman, Merna R. Villarejo, Structural and catalytic properties of peptidase N from Escherichia coli K-12 Archives of Biochemistry and Biophysics. ,vol. 213, pp. 384- 394 ,(1982) , 10.1016/0003-9861(82)90564-1
Timo Stressler, Thomas Eisele, Claudia Baur, Julia Wangler, Andreas Kuhn, Lutz Fischer, Extracellular peptidases from insect- and compost-associated microorganisms: screening and usage for wheat gluten hydrolysis European Food Research and Technology. ,vol. 241, pp. 263- 274 ,(2015) , 10.1007/S00217-015-2452-8
Israel Schechter, Arieh Berger, On the size of the active site in proteases. I. Papain Biochemical and Biophysical Research Communications. ,vol. 27, pp. 157- 162 ,(1967) , 10.1016/S0006-291X(67)80055-X
J SURH, E DECKER, D MCCLEMENTS, Influence of pH and Pectin Type on Properties and Stability of Sodium-Caseinate Stabilized Oil-in-Water Emulsions Food Hydrocolloids. ,vol. 20, pp. 607- 618 ,(2006) , 10.1016/J.FOODHYD.2005.07.004
Nooshin Alizadeh-Pasdar, Eunice C. Y. Li-Chan, Comparison of protein surface hydrophobicity measured at various pH values using three different fluorescent probes. Journal of Agricultural and Food Chemistry. ,vol. 48, pp. 328- 334 ,(2000) , 10.1021/JF990393P
Timo Stressler, Thomas Eisele, Lutz Fischer, Simultaneous monitoring of twelve angiotensin I converting enzyme inhibitory peptides during enzymatic β-casein hydrolysis using Lactobacillus peptidases International Dairy Journal. ,vol. 30, pp. 96- 102 ,(2013) , 10.1016/J.IDAIRYJ.2012.12.003