Properties and uses of protein hydrolysates (Review)

Properties of protein hydrolysates and possible uses of these substances in research and various branches of industry are considered. The main problem discussed in this paper is the relationship between the degree of protein conversion and characteristics (structural-functional and physicochemical) of hydrolysates.     

Isolation and Characterization of Immobilized Aminoacylase from Streptoverticillium olivoreticuli

Immobilization of aminoacylase from Streptoverticillium olivoreticuli by incorporation into acrylamide gel has been investigated. The data showed that the process should be carried out at constant pH. Thermal inactivation of the immobilized enzyme under the reaction conditions was studied. The kinetics of enzymatic stereospecific deacylation of N-acetyl-DL-phenylalanine was analyzed. The results of this study may be used in the synthesis of amino acid enantiomers.     

Intensification of composting processes by aerobic microorganisms: A review

Microbiological and biotechnological characteristics of intensification of aerobic processing of organic waste have been reviewed, with a view for revealing two types of correlations: (1) between the quality of the composts obtained and the microorganisms involved in composting and (2) between physicochemical parameters and consumer properties of the composts.     

A cephalexin-synthesizing hydrolase fromXanthomonas rubrilineans

The use of peptide hydrolase (EC 3.4.13.1) fromXanthomonas rubrilineans for synthesis of the antibiotic cephalexin from 7-aminodesacetoxycephalosporanic acid was studied. The optimum conditions for production of cephalexin were determined, and the yield exceeded 80%. A method for monitoring the synthesis of this antibiotic by means of a conventional amino acid analyzer is proposed.     

Production and purification of protein hydrolysates (review)

Recent achievements in the technology of producing protein hydrolysates are reviewed. Approaches to describing the mechanism of hydrolysis and the possibility of purifying hydrolysates for their use in the food, medical, forage, and microbiological industries are discussed.     

Comparison of proteolytic activities of the enzyme complex from mammalian pancreas and pancreatin

The proteolytic activity and thermal stability of the enzyme complex of a cell suspension from pig and bovine pancreas glands was compared with those of pancreatin. The enzyme complex displayed the highest thermal stability and activity at 50°C. The kinetic constants, energies of activation and inactivation of the enzyme complex, and pH optimum (7.0 ± 0.1) at which this complex had the maximum proteolytic activity were determined. Pancreatin had a pH optimum of 8.0 ±0.1.     

Aerobic processing of organic waste into composts

The current achievements in the field of aerobic waste processing into composts are reviewed, with an emphasis on amelioration of the environment and targeted use for intensification of agriculture. The methods for obtaining microbiological transformation products of household, agricultural, and industrial waste and their characteristics are analyzed.     

The Kinetics of Hydrolysis of Animal Fat by Pancreatic Lipase

Hydrolysis of lipids from beef fat by pancreatic lipase was studied. The maximum release of free fatty acids was shown to occur at 40°C for the first 3 h of the experiment. After this, transetherification was predominant. The main kinetic parameters were the following: maximum hydrolysis rate, V = 1.25 ± 0.1 mg fat/ml min; Michaelis constant, K _M ^H = 100 ± 12 mg fat/ml; constant of substrate inhibition, K _S = 10.0 ± 0.8 mg fat/ml; equilibrium constant, K _P = 277 ± 170 mg fat/ml; and activation energy of beef fat hydrolysis by pancreatic lipase, E _a = 19.1 ± 1.1 kJ/mole. The kinetic method used could be applied to development of the method for biotransformation of poorly assimilated fats into more valuable products.     

Collagen Fractions Obtained by Water–Salt Extraction from Raw Materials of Animal Origin

Collagen fractions have been isolated by water–salt extraction from raw materials of animal origin (various tendon types or subcutaneous tissues of cattle or porcine skin). Collagen fractions with maximum capacity for water and fat retention were isolated with high efficiency by water–salt solutions containing 1–10% sodium chloride at temperatures below 50°C. The values of the effective constant of extraction rate (min^–1) at pH 6.5, 9.0, and 12.0 were equal to (2.7 ± 0.1) × 10^–3, (6.2 ± 0.5) × 10^–3, and (15.4 ± 0.7) × 10^–3, respectively. The optimum conditions found made it possible to isolate from collagen those proteinaceous fractions that are of practical use in food industry.