Continuous enzymatic hydrolysis of beta-casein and isoelectric collection of some of the biologically active peptides in an electric field

Biotechnology Progress
P G RighettiM Mortarino

Abstract

Among the milk proteins, bovine beta-casein has the peculiarity of containing in its sequence some peptides liable to interfere in mineral nutrition and some peptides with opioid (casomorphines), antihypertensive, and immunomodulatory activities. In this work we propose a novel type of multicompartment enzyme reactor, operating under an electric field, for the continuous hydrolysis of milk proteins such as beta-casein. The enzyme trypsin is trapped, with zwitterionic buffering ions and its substrate beta-casein, in solution between two isoelectric membranes having pI values encompassing the isoelectric point of the enzyme. Additionally, beta-casein is captured inside the same reaction chamber with the aid of sieving membranes, since its pI is too far away from the pI of trypsin. This setup permits the continuous operation at the pH of optimum of activity. The peptides, arising from tryptic hydrolysis of beta-casein, are removed under the influence of the electric field and collected in different chambers in which they are isoelectric and isoionic as well. The purity of the peptides collected is ascertained by capillary zone electrophoresis and their identity confirmed by N-terminal sequencing and MALDI-TOF mass spectrometry. Th...Continue Reading

Citations

Jun 1, 2001·Journal of Biochemical and Biophysical Methods·M CretichG Carrea
Aug 1, 2014·Critical Reviews in Food Science and Nutrition·Duc Doan NguyenVicky Ann Solah
Dec 6, 2003·Analytical and Bioanalytical Chemistry·A BossiP G Righetti
Jul 14, 1998·Electrophoresis·P G Righetti, A Bossi
Jan 27, 2019·Current Protein & Peptide Science·Fengtao MaPeng Sun
Jan 24, 2002·Journal of Agricultural and Food Chemistry·Paule Emilie GroleauYves Pouliot

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