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  • 1
    Electronic Resource
    Electronic Resource
    Enzymatic hydrolysis of whey proteins: I. Kinetic models (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 44 (1994), S. 523-528 
    Details
    ISSN: 0006-3592
    Keywords: whey proteins ; proteases ; enzymatic hydrolysis ; peptides ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: We have studied the enzymatic hydrolysis of whey proteins at pH 8 and50°C with two proteases of bacterial origin, MKC Protease 660 L, and one of animal origin, PEM 2500 S. Our results show that a greater degree of hydrolysis is achieved under the same experimental conditions with the bacterial proteases than with the animal one. In our interpretation of the results we propose a mechanism in which the hydrolytic reaction is a zero-order one for the substrate, and the enzyme denaturalizes simultaneously via a second-order kinetic process due to free enzyme attacking enzyme bound to the substrate. Our results also indicate that there is an irreversible serine-protease inhibitor in whey proteins. © 1994 John Wiley & Sons, Inc.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260440415
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Enzymatic hydrolysis of whey proteins. II. Molecular-weight range (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 44 (1994), S. 529-532 
    Details
    ISSN: 0006-3592
    Keywords: whey proteins ; proteases ; enzymatic hydrolysis ; peptides ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Using high-pressure liquid chromatography we studied the distribution of molecular weights in whey-protein hydrolysates using the following commercially obtained proteases: Alcalasa 0.6 L and Protease 660 L, both bacterial in origin, and PEM 2500 S, of animal origin. In each of the systems, the range of molecular weights in the hydrolysate depended solely on the degree of hydrolysis (DH) achieved. For DH ≥ 20, between 65% and 95% of the hydrolysate is made up of peptides with a molecular weight of less than 1,000 Da. © 1994 John Wiley & Sons, Inc.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260440416
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    A simple method for obtaining kinetic equations to describe the enzymatic hydrolysis of biopolymers (1996)
    Chichester : Wiley-Blackwell
    Journal of Chemical Technology AND Biotechnology 67 (1996), S. 286-290 
    Details
    ISSN: 0268-2575
    Keywords: kinetic ; spline functions ; biopolymers ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: A procedure to obtain the overall rate of hydrolysis of biopolymers is proposed, based on the fitting of the experimental data x = f(t) to cubic spline functions and from these, by differentiation, to obtain dx/dt. The values of these dx/dt slopes are an exclusive function of the conversion, x, when E0, S0, pH and temperature are constant. The fitting of dx/dt versus x leads to equations of the type \documentclass{article}\pagestyle{empty}\begin{document}$$\frac{{dx}}{{dt}} = a \cdot x\exp(- b \cdot x)$$\end{document} for the glucoamylase-starch system, where b = 8·75 and a = f(E0, T).
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
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