Structural organization of the rat acyl-peptide hydrolase gene.
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Preparation of medical protein hydrolysates with the use of complete hydrolysis of proteins by bacterial enzyme complexes, such as protosubtilin G10x and bacterial peptidase immobilized on aminosilylated alumina was shown to be possible. The activity, thermostability and substrate specificity of the heterogeneous biocatalysts were studied. The integral kinetics of the hydrolysis of sodium caseinate and peptides included in partial acid and enzymatic casein hydrolyzates and blood was investigated. The engineering approaches to mathematical simulation of the bioproteolysis kinetics and the results of their use in processing of the experimental data are discussed.
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