Chymotrypsin selectively digests β-lactoglobulin in whey protein isolate away from enzyme optimal conditions: potential for native α-lactalbumin purification.

@article{Lisak2013ChymotrypsinSD,
  title={Chymotrypsin selectively digests β-lactoglobulin in whey protein isolate away from enzyme optimal conditions: potential for native α-lactalbumin purification.},
  author={Katarina Lisak and Jos{\'e} Toro-Sierra and Ulrich Kulozik and Rajka Bo{\vz}ani{\'c} and Seronei Chelulei Cheison},
  journal={The Journal of dairy research},
  year={2013},
  volume={80 1},
  pages={14-20}
}
The present study examines the resistance of the α-lactalbumin to α-chymotrypsin (EC 3.4.21.1) digestion under various experimental conditions. Whey protein isolate (WPI) was hydrolysed using randomised hydrolysis conditions (5 and 10% of WPI; pH 7.0, 7.8 and 8.5; temperature 25, 37 and 50 °C; enzyme-to-substrate ratio, E/S, of 0.1%, 0.5 and 1%). Reversed-phase high performance liquid chromatography (RP-HPLC) was used to analyse residual proteins. Heat, pH adjustment and two inhibitors (Bowman… CONTINUE READING

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