Enzymatic Generation of Peptides from Potato Proteins by Selected Proteases and Characterization of their Structural properties

摘要: The use of low grade starting material for the generation peptides with bioactivity properties is interest. proteins from potato starch industry byproduct a promising source, as several health benefits may be associated their hydrolysates. efficiency selected proteases (Novo Pro-D, Alcalase, Flavourzyme, and Papain), exhibiting different substrate specificities cleavage action modes, to hydrolyze protein isolate (patatin protease inhibitors) was investigated. Novo Pro-D resulted in lowest degree hydrolysis, whereas Papain exhibited high catalytic hydrolysis proteins. behaved concentration dependent manner. However, end-product profile (peptides free amino acids) not only on specificity, its mode (endo/exo) availability intermediate substrates but also contribution inhibitors reaction kinetics through inhibitory effects. Indeed, dependence exo-activity endo-action shown significant. generated more unique peptide sequences homology assessment matching when compared Flavourzyme. This can attributed exo-peptidase activity Flavourzyme resulting shorter which were difficult match. produced originated patatin fraction, release corresponding inhibitor fractions. © 2016 American Institute Chemical Engineers Biotechnol. Prog., 32:420-429, 2016.