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5527689 Enzymatic coupling of L-phenylalanine methyl ester and N-benzyloxycarbonyl-aspartic acid
PATENT ABSTRACTS
5527689 ENZYMATIC COUPLING OF L-PHENYLALANINE METHYL ESTER AND N-BENZYLOXYCARBONYL-AS PARTIC ACID Irino Shigeaki; Nakamura Shin-ichiro; Oyama Kiyotaka; Quaedflieg Peter J L M; Van Dooren Theodorus J G M Yamaguchi, JAPAN assigned to Holland Sweetener Company V o F The invention relates to a process for the preparation of N-benzyloxycarbonylalpha-L-aspartyl-L-phenylalanine methyl ester by enzymatic coupling of N-benzyloxycarbonyl-L-aspartic acid and L-phenylalanine methyl ester in an aqueous medium with formation of a precipitate, the coupling reaction being effected with (virtually) equimolar quantities of N-benzyloxycarbonylL-aspartic acid and L-phenylalanine methyl ester under the influence of a neutral protease at an initial pH of from 4.5 to 6.0 and in the presence of from 3 to 25’%,calculated as per cent by weight based on the total reaction mixture, of an alkali metal salt, alkaline earth metal salt or ammonium salt.
5527698 RECOMBINANT PHOSPHOLIPASE A2 ENZYME Knopf John L; Clark Jame Acton, MA, UNITED STATES assigned to Genetics Institute Inc The invention provides novel DNA and peptide sequences encoding a family of phospholipase A2 enzymes, with specific activities of approximately 20 mumol/min/mg in the mixed micelle assay. These enzymes are useful in methods for
217
detecting the anti-inflammatory potential of various chemical agents. The invention also details novel methods for determining such potential using the novel sequences, methods for making the novel peptides, and methods for developing new anti-inflammatory drugs,
5527699 MALTOHEXAOSE AND MALTOHEPTAOSE-FORMING AMYLASE FROM A MICROORGANISM Nakano Masayuki; Chaen Hiroto; Sugimoto Toshiyuki; Miyake Toshio Okayama, JAPAN assigned to Kabushiki Kaisha Hayashibara Seibutsu Kagaku Kenkyujo An amylase is preferrably obtained from Alcaligenes latus FERM BP-4578. The amylase has an activity of mainly forming maltohexaose and maltoheptaose from starch, but does not substantially have an activity of hydrolyzing maltohexaose and an oligosaccharide having a molecular weight lower than maltohexaose. The amylase does not substantially act on maltoheptaose and has a molecular weight of about 43,000+3,000 daltons as measured by sodium dodecyl sulfate polyacrylamide gel electrophoresis. It has an isoelectric point of about 7.6+0.5 as measured on isoelectrophoresis using an ampholyte, an optimum pH of about 5.0 in the presence of calcium ion, an optimum temperature of about 70 degrees C. in the presence of calcium ion as measured in terms of relative enzyme activity, a pH stability of about 4.5-10.5 in the presence of calcium ion and a thermal stability up to about 60 degrees C. in the presence of calcium ion as measured in terms of residual enzyme activity. By using the amylase, saccharide compositions rich in maltohexaose and/or maltoheptaose or those rich in maltohexaitol and/or
5527689 ENZYMATIC COUPLING OF L-PHENYLALANINE METHYL ESTER AND N-BENZYLOXYCARBONYL-AS PARTIC ACID Irino Shigeaki; Nakamura Shin-ichiro; Oyama Kiyotaka; Quaedflieg Peter J L M; Van Dooren Theodorus J G M Yamaguchi, JAPAN assigned to Holland Sweetener Company V o F The invention relates to a process for the preparation of N-benzyloxycarbonylalpha-L-aspartyl-L-phenylalanine methyl ester by enzymatic coupling of N-benzyloxycarbonyl-L-aspartic acid and L-phenylalanine methyl ester in an aqueous medium with formation of a precipitate, the coupling reaction being effected with (virtually) equimolar quantities of N-benzyloxycarbonylL-aspartic acid and L-phenylalanine methyl ester under the influence of a neutral protease at an initial pH of from 4.5 to 6.0 and in the presence of from 3 to 25’%,calculated as per cent by weight based on the total reaction mixture, of an alkali metal salt, alkaline earth metal salt or ammonium salt.
5527698 RECOMBINANT PHOSPHOLIPASE A2 ENZYME Knopf John L; Clark Jame Acton, MA, UNITED STATES assigned to Genetics Institute Inc The invention provides novel DNA and peptide sequences encoding a family of phospholipase A2 enzymes, with specific activities of approximately 20 mumol/min/mg in the mixed micelle assay. These enzymes are useful in methods for
217
detecting the anti-inflammatory potential of various chemical agents. The invention also details novel methods for determining such potential using the novel sequences, methods for making the novel peptides, and methods for developing new anti-inflammatory drugs,
5527699 MALTOHEXAOSE AND MALTOHEPTAOSE-FORMING AMYLASE FROM A MICROORGANISM Nakano Masayuki; Chaen Hiroto; Sugimoto Toshiyuki; Miyake Toshio Okayama, JAPAN assigned to Kabushiki Kaisha Hayashibara Seibutsu Kagaku Kenkyujo An amylase is preferrably obtained from Alcaligenes latus FERM BP-4578. The amylase has an activity of mainly forming maltohexaose and maltoheptaose from starch, but does not substantially have an activity of hydrolyzing maltohexaose and an oligosaccharide having a molecular weight lower than maltohexaose. The amylase does not substantially act on maltoheptaose and has a molecular weight of about 43,000+3,000 daltons as measured by sodium dodecyl sulfate polyacrylamide gel electrophoresis. It has an isoelectric point of about 7.6+0.5 as measured on isoelectrophoresis using an ampholyte, an optimum pH of about 5.0 in the presence of calcium ion, an optimum temperature of about 70 degrees C. in the presence of calcium ion as measured in terms of relative enzyme activity, a pH stability of about 4.5-10.5 in the presence of calcium ion and a thermal stability up to about 60 degrees C. in the presence of calcium ion as measured in terms of residual enzyme activity. By using the amylase, saccharide compositions rich in maltohexaose and/or maltoheptaose or those rich in maltohexaitol and/or