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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 44 (1994), S. 523-528 
    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
    Library Location Call Number Volume/Issue/Year Availability
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  • 2
    Electronic Resource
    Electronic Resource
    Chichester : Wiley-Blackwell
    Journal of Chemical Technology AND Biotechnology 67 (1996), S. 350-356 
    ISSN: 0268-2575
    Keywords: acid hydrolysis ; pretreatments ; cellulose ; cellulose solubilization ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: The effects of temperature (25-40°C), H2SO4 concentration (31-70% (w/v)) and the acid/substrate relationship (1-5 cm3 of H2SO4 per g-1 of cellulose) on the solubilization rate of microcrystalline cellulose and on the glucose production rate have been analysed. The solubilization process was by determining reducing groups present in solution. For acid/substrate relationships of more than 1 cm3 g-1 and H2SO4 concentrations of greater than 62% (w/v), the acid promoted the total solubilization of the cellulose in the form of chains with a low degree of polymerization within 4 h. The solubilization demonstrated zero-order kinetics in which the specific rate and time of total solubilization are a function of the variables in operation. Glucose was produced according to a mechanism of two consecutive first-order pseudo-homogeneous reactions. The values of the kinetic constants k1 and k2 have been correlated with temperature, the H2SO4 concentration and the acid/substrate relationship.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Chichester : Wiley-Blackwell
    Journal of Chemical Technology AND Biotechnology 67 (1996), S. 286-290 
    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
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