Control of the degree of hydrolysis of a protein modification with immobilized protease by the pH-drop method
β Scribed by S. J. Ge; L. X. Zhang
- Publisher
- John Wiley and Sons
- Year
- 1993
- Tongue
- English
- Weight
- 452 KB
- Volume
- 13
- Category
- Article
- ISSN
- 0138-4988
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β¦ Synopsis
Abstract
A mathematical model, DH = 1/k(10^β2ΞpH^ β 1), between the pHβdrop (ΞpH) and degree of hydrolysis (DH) of an enzymatic modification of casein was developed to assess the DH in a packedβbed column reactor by directly monitoring the pH value of the modified protein system. It was demonstrated that the linear DH range and the k value of the equation were dependent on the reactor type and the specificity of the proteolytic enzymes immobilized on chitin used in the present study, but no effect of the substrate casein concentration on the linear DH range was observed. Since DH and ΞpH values of the modified casein correlated with the flow rate in a packedβbed column reactor, it was suggested that the DH value, in a considerably wide range of casein modification with a certain immobilized protease in a column reactor, could be controlled by adjusting the flow rate of the substrate and monitored by a pHβmeter. This relationship might be used as a basis for scaleβup and longβterm operation of enzymatic modification of proteins by immobilized protease in a column reactor.
π SIMILAR VOLUMES
Kat serum IPG-Dalt after solvent inhalation 655 strate these differences the staining reaction shown in Fig. was intentionally extended, with resultant impaired resolution of strongly reacting isoforms from A. nodosum (lane 1). Additionally, Fig. demonstrates a positive reaction of all isoenzymes