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Preparation of protein hydrolysates with the use of immobilized bacterial peptide hydrolases


, : Preparation of protein hydrolysates with the use of immobilized bacterial peptide hydrolases. Antibiotiki i Meditsinskaya Biotekhnologiya 30(4): 243-249

The 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, is possible. The activity, thermostability and substrate specifity of the heterogenous biocatalysts were studied. The integral kinetics of the hydrolysis of sodium caseinate and peptides included in partial acid and enzymatic casein hydrolysates 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.


Accession: 006173729

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Related references

Neklyudov, A.D.; Navashin, S.M.; Bartoshevich, Y.E.; Tsibanov, V.V., 1985: Preparation of protein hydrolysates using immobilized peptide hydrolases. A mathematical model was used to study the kinetics of complete hydrolysis of sodium caseinate and peptide mixtures by protosubtilin G10X and bacterial peptidase immobilized on aminosilylated alumina. After correction, the model accurately describ...

Nekliudov, A.D.; Navashin, S.M.; Bartoshevich, I.E.; Tsibanov, V.V., 1985: Isolation of protein hydrolysates by using immobilized bacterial peptide hydrolases. 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 activ...

Nekliudov, A.D.; Deniakina, E.K., 2004: Hydrolysis of peptides by immobilized bacterial peptide hydrolases. The feasibility of hydrolysis of a mixture of peptides with an enzyme from the bacterium Xanthomonas rubrilineans, displaying a peptidase activity and immobilized on aluminum oxide, was studied. Kinetic schemes and equations allowing for approachi...

Engel, H.; Van Leeuwen, A.; Dijkstra, A.; Keck, W., 1992: Enzymatic preparation of 1,6-anhydromuropeptides by immobilized murein hydrolases from Escherichia coli fused to staphylococcal protein A. In order to produce biologically active 1,6-anhydro-muropeptides in large amounts by enzymatic degradation of isolated bacterial murein polymer highly specific periplasmic murein-metabolizing enzymes from Escherichia coli are made available. The r...

Engel, H.; van Leeuwen, A.; Dijkstra, A.; Keck, W., 1992: Enzymatic preparation of 1,6-anhydro-muropeptides by immobilized murein hydrolases from Escherichia coli fused to staphylococcal protein A. In order to produce biologically active 1,6-anhydro-muropeptides in large amounts by enzymatic degradation of isolated bacterial murein polymer highly specific periplasmic murein-metabolizing enzymes from Escherichia coli are made available. The g...

Anonymous, 1986: Functional protein hydrolysates a process for their preparation use of these protein hydrolysates as a food additive and foods containing these proteins hydrolyzed us patent 4627983 dec 9 1986

Ledvina M.; L.B.lla F.S., 1971: Fluorescent substances in protein hydrolysates part 2 comparison of some protein and peptide hydrolysates. Canadian Journal of Biochemistry 49(1): 6-11

Franek, F.; Hohenwarter, O.; Katinger, H., 2000: Plant protein hydrolysates: preparation of defined peptide fractions promoting growth and production in animal cells cultures. A new approach was applied with the aim at producing plant protein hydrolysates less heterogeneous and less contaminated with nonpeptide substances than are the presently available digests. A significant reduction of nonprotein contaminants was ac...

Silvestre, M.P.C.; Hamon, M.; Yvon, M., 1994: Analysis of protein hydrolysates. 2. Characterization of casein hydrolysates by a rapid peptide quantification method. Casein hydrolysates prepared in the laboratory or purchased from a manufacturer were characterized for the proportion of amino acids in free form, in short-chain (di- and tripeptides) or larger peptides. The hydrolysates were fractionated by size...

Ledvina, M.; LaBella, F.S., 1971: Fluorescent substances in protein hydrolysates. II. Comparison of some protein and peptide hydrolysates. Canadian Journal of Biochemistry 49(1): 6-11