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We have studied the enzymatic hydrolysis of whey proteins at pH 8 and50 degrees 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. (c) 1994 John Wiley & Sons, Inc.

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.

We study the enzymatic hydrolysis of lactose by a commercial enzyme from a selected strain of Kluyveromyces fragilis. The variables analyzed were: temperature (25-40 • C), enzyme concentration (0.1-3.0 g l −1 ), lactose concentration (0.0278-0.208 M), and initial galactose concentration (0.0347 M). On the basis of the data analyzed, both published and in the present work, we propose a Michaelis-Menten kinetic model with inhibition by the product (galactose), which reveals that the substrate (lactose) and the product (galactose) present similar affinity for the active site of the enzyme.

A commercial lipase (E.C. 3.1.1.3) from Thermomyces lanuginosus was studied in order to assess its interaction with commercial nonionic (Findet Ò 1214N/16, Findet 1214N/23 and Glucopon Ò 650) and anionic (linear alkylbenzene sulphonate; LAS) surfactants, as well as the cleaning action exerted by the enzyme on hard surfaces. Nonionic surfactants seem to prevent or delay enzyme penetration at the interface, thereby decreasing lipase activity. Notably, no inhibitory effect of the anionic surfactant LAS on lipase action was found, higher conversions being achieved after 20 min of enzymatic hydrolysis in the presence of this surfactant than in its absence. A device for testing detersive performance, the so-called bath-substrateflow, was used in washing experiments with the lipase at different temperatures with or without surfactant. Employing two different oily stains (tributyrin and triolein), it was found that the lipase by itself increases detergency significantly, preventing the subsequent redeposition of the removed dirt. Expressions relating detersive efficiency to lipase concentration and temperature were obtained using ''Statistical Design of Experiments'' methodology.

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One of the most studied approaches in solubilization of insoluble phosphates is the biological treatment of rock phosphates. In recent years, various techniques for rock phosphate solubilization have been proposed, with increasing emphasis on application of P-solubilizing microorganisms. The P-solubilizing activity is determined by the microbial biochemical ability to produce and release metabolites with metal-chelating functions. In a number of studies, we have shown that agro-industrial wastes can be efficiently used as substrates in solubilization of phosphate rocks. These processes were carried out employing various technologies including solid-state and submerged fermentations including immobilized cells. The review paper deals critically with several novel trends in exploring various properties of the above microbial/agro-wastes/rock phosphate systems. The major idea is to describe how a single P-solubilizing microorganism manifests wide range of metabolic abilities in different environments. In fermentation conditions, P-solubilizing microorganisms were found to produce various enzymes, siderophores, and plant hormones. Further introduction of the resulting biotechnological products into soil-plant systems resulted in significantly higher plant growth, enhanced soil properties, and biological (including biocontrol) activity. Application of these bio-products in bioremediation of disturbed (heavy metal contaminated and desertified) soils is based on another important part of their multifunctional properties.