Acylase Activity Research Articles

Studies on Acylase Activity and Microorganisms. XIV. A Certain Strain of Soil Bacteria capable of resolving Lysine by its Metabolism on α-N-Phenylacetyl-ε-N-benzoyl-DL-lysine

A certain strain (KT-311) isolated from soil had the metabolic activity shown in Table I and could metabolize α-N-phenylacetyl-e-N-benzoyl-DL-lysine to produce e-N-benzoyl-L-lysine and α-N-phenylacetyl-e-N-benzoyl-D-lysine in good yield. KT-311 could hydrolyse phenylacetyl derivative but not benzoyl derivative of e-N-benzoyl-L-lysine. KT-311 seemingly belongs to the Pseudomonas group.

Studies on Acylase Activity and Microorganisms. XIII. Optical Resolution of p-Methoxyphenylalanine and 3, 4-Methylenedioxyphenylalanine by Metabolism of Soil Bacteria on Benzoyl Derivatives of DL-Amino Acids

The metabolic activities of KT-231 and KT-230 were tested on p-methoxyphenylalanine and 3, 4-methylenedioxyphenylalanine and their benzoyl derivatives (Table I). It was demonstrated that one strain (KT-231) of soil bacteria metabolized benzoyl derivatives of p-methoxy-DL-phenylalanine and 3, 4-methylenedioxy-DL-phenylalanine to produce L-amino acids and the corresponding benzoyl-D-amino acids.

Studies on Acylase Activity and Microorganisms. XI. A New Method for resolving DL-Amino Acids by Metabolism of Soil Bacteria.

Studies on Acylase Activity and Microorganisms. XI. A New Method for resolving DL-Amino Acids by Metabolism of Soil Bacteria.

Studies on Acylase Activity and Microorganisms. XII. Optical Resolution of Glutamic and Aspartic Acids by Metabolism of Soil Bacteria on Benzoyl Derivatives of DL-Amino Acids

Studies on Acylase Activity and Microorganisms. XII. Optical Resolution of Glutamic and Aspartic Acids by Metabolism of Soil Bacteria on Benzoyl Derivatives of DL-Amino Acids

Studies on Amino Acids XII

(1) The occurrence of acylase activity in plants such as vegetables, pulses, cereals, pota-toes, fruits and mushroom, has been confirmed for the first time. (2) Of the acyl and glycyl amino acids tested, acetylmethionine and glycylmethionine were most readily hydrolyzed by most of the plant preparations tested, and susceptibility was lowered in the order of chloroacetylphenyl-alanine, acetylglutamic acid and ε-benzoyl-α-acetyllysine. The last mentioned compound was insusceptible to the plant acylase except in the case of mushroom. (3) In the germination state of cereals and pulses, higher activities, although not so appa-rent, were often observed. (4) Mushroom showed higher and some-what different hydrolytic activities than the other higher plants tested.

Studies on Amino Acids. XI.

As a part of the studies intending to clarify biological significance of the presence of acylase, enzymatic activity which hydrolyzes acyl amino acids, its activity in yeast was investigated. As a results, the occurrence in yeast of acylase activity was confirmed for the first time.In order to study the enzymatic properties of this acylase activity, experiments were carried out with the enzyme preparation from brewer’s yeast. As a result of the investigation, yeast acylase was found to be able to hydrolyze a number of acyl amino acids, of these chloroacetyl derivatives especially readily, as in the case of previously studied acylase activity in other sources such as mold acylase. Several observations on the influence of metal ions and inhibitors, optical specificity and others were also presented.

Studies on Amino Acids. XI

As a part of the studies intending to clarify biological significance of the presence of acylase, enzymatic activity which hydrolyzes acyl amino acids, its activity in yeast was investigated. As 4 results, the occurrence in yeast of acylase activity was confirmed for the first time. In order to study the enzymatic properties of this acylase activity, experiments were carried out with the enzyme preparation from brewer's yeast. As a result of the investigation, yeast acylase was found to be able to hydrolyze a number of acyl amino acids, of these chloroacetyl derivatives especially readily, as in the case of previously studied acylase activity in other sources such as mold acylase. Several observations on the influence of metal ions and inhibitors, optical specificity and others were also presented.

Studies on Amino Acids. X

The growth studies of methionine requiring mutant of Escherichia coli disclosed that several acyl methionines were utilized by the mutants. Furthermore, the cell-free extracts of Escherichia coli and Aerobacter aerogenes were found to show almost equal hydrolytic activity towards acyl amino acids. In order to find the enzymatic properties of the acylase activity, the experiments were carried out with the alcohol-fractionated extracts of the acetone-dried cells of Escherichia coli K-12. As a result of the investigation, acylase activity of the preparation from Escherichia coli was found to be lower and also a lesser number of acyl amino acids were hydrolyzed than the mold acylase which had been previously studied by the authors. Activation by cobalt ion and several other observation were also presented.

微生物におけるアシラーゼ能の研究 (第2報)

微生物におけるアシラーゼ能の研究 (第2報)

微生物に於けるアシラーゼ能の研究 (第7報)

微生物に於けるアシラーゼ能の研究 (第7報)

Studies on acylase activity and microorganisms. VIII. Enzymatic hydrolysis of 6-N-benzoyl-L-lysine.

Studies on acylase activity and microorganisms. VIII. Enzymatic hydrolysis of 6-N-benzoyl-L-lysine.

Studies on Acylase Activity and Microorganisms. X. Enzymatic Resolution of Alloisoleucine by Soil Bacteria, KT 85 (Pseudomonas sp.).

A strain of soil bacteria, KT 85 (Pseudomonas sp.), asymmetrically hydrolyzed N-acetyl-DL-alloisoleucine to give L-alloisoleucine and N-acetyl-D-alloisoleucine in a good yield.

Studies on Amino Acids. X

The growth studies of methionine requiring mutant of Escherichia coli disclosed that several acyl methionines were utilized by the mutants. Furthermore, the cell-free extracts of Escherichia coli and Aerobacter aerogenes were found to show almost equal hydrolytic activity towards acyl amino acids.In order to find the enzymatic properties of the acylase activity, the experiments were carried out with the alcohol-fractionated extracts of the acetone-dried cells of Escherichia coli K-12. As a result of the investigation, acylase activity of the preparation from Escherichia coli was found to be lower and also a lesser number of acyl amino acids were hydrolyzed than the mold acylase which had been previously studied by the authors. Activation by cobalt ion and several other observation were also presented.

Studies on acylase activity and microorganisms. IX. Enzymatic resolution of tryptophan by a strain of soil bacteria.

Studies on acylase activity and microorganisms. IX. Enzymatic resolution of tryptophan by a strain of soil bacteria.

DL-アミノ酸の酵素による光学的分割

A survey of mold strains for the acylase property of asymmetric hydrolysis of N-acylated DL-amino acids was undertaken. Hundred and nineteen strains of Aspergillus and twenty strains of Penicillium were cultured on solid medium, wheat bran, and the extracts of the culture medium were assayed for the acylase activity. Acetyl-DL-glutamic acid hydrolysis test with the acylase was conducted by 24 hrs. incubation at pH 5.8 and 37° The procedure of determination of the liberated amino acid was modified from the method of STEIN and MOORE and the activity was expressed by the amount of the liberated amino acid (Table 2). A number of strains of Aspergillus and several strains of Penicillium produced sufficient acylase activity. The greatest activity was obtained by five strains of A. tamarii and each strain of A. cryzae, P. vinaceous, P. oxalicum var. pectinopcrum nov. and P. corymbiferum. The presence of calcium carbonate in the survey medium for Penicillium was found to be necessary for enzyme production to prevent the pH drop of the medium and to result the greatest enzyme yields (Table 1).