ISSN:
1745-4514
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Process Engineering, Biotechnology, Nutrition Technology
Notes:
β-Lactoglobulin was esterified with methanol, ethanol or propanol, yielding 100, 60 and 44% esterification, respectively. The kinetics of peptic hydrolysis of unmodified, methylated-, ethylated-and propylated-fi-lactoghbulin derivatives were followed under various conditions of time, temperature, and enzyme and protein concentrations. The resulting hydrolysates were analyzed by SDS-PAGE and RP-HPLC. Changes of temperature and enzyme concentration influenced strongly the rate of hydrolysis and the RP-HPLC profiles while protein concentration had much smaller impact on reaction rates when tested in the range2.5–20mg/mL. Peptic hydrolysis of methylated-β-lactoglobulin derivatives could proceed at a temperature as low as 4C and at an enzyme/substrate ratio as low as 0.125%, Peptide profiles of the hydrofysates of methyl- and ethyl-β-lactoglobulin derivatives were gemratty quite similar except for the appearance of additional peaks in case of methyl-p-lactoglobulin. RP-HPLC profile of propyl-β-lactoglobulin ester was slightly different from that of both the methyl-and ethyl-β-lactoglobulin. The features of the peptide profiles of the different hydrolysates of esterified β-lactoglobulin did not differ after long pepsinofysis. The population of small hydrophilic peptide increased, accompanied by a decrease of the large hydrophobic peptides (for methyl derivative) and the hydrolysis of intact protein (for ethyl- and propyl-derivatives).
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1745-4514.2001.tb00733.x
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