{"title":"青霉素G酰化酶拆分dl -苯甘氨酸。","authors":"R S Kulkarni, U R Kalkote","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>The parameters for complete hydrolysis of L-phenyl acetyl phenylglycine (L-PAPG) using immobilized penicillin G acylase (IMEPGA) were investigated. IMEPGA exhibited maximum activity at pH 8.5 and 50 degrees C. The apparent Km value observed was 10 mM. Quantitative hydrolysis (>97%) of the L-PAPG was achieved within 45 min, at pH 7.8 and 37 degrees C, when 0.5% (w/v) of DL-PAPG was used and the concentration of IMEPGA was 133 IU/gm of DL-PAPG. The IMEPGA was used for 50 cycles.</p>","PeriodicalId":12923,"journal":{"name":"Hindustan antibiotics bulletin","volume":"47-48 1-4","pages":"41-4"},"PeriodicalIF":0.0000,"publicationDate":"2005-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Resolution of DL-Phenylglycine by Penicillin G acylase.\",\"authors\":\"R S Kulkarni, U R Kalkote\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The parameters for complete hydrolysis of L-phenyl acetyl phenylglycine (L-PAPG) using immobilized penicillin G acylase (IMEPGA) were investigated. IMEPGA exhibited maximum activity at pH 8.5 and 50 degrees C. The apparent Km value observed was 10 mM. Quantitative hydrolysis (>97%) of the L-PAPG was achieved within 45 min, at pH 7.8 and 37 degrees C, when 0.5% (w/v) of DL-PAPG was used and the concentration of IMEPGA was 133 IU/gm of DL-PAPG. The IMEPGA was used for 50 cycles.</p>\",\"PeriodicalId\":12923,\"journal\":{\"name\":\"Hindustan antibiotics bulletin\",\"volume\":\"47-48 1-4\",\"pages\":\"41-4\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2005-02-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Hindustan antibiotics bulletin\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Hindustan antibiotics bulletin","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Resolution of DL-Phenylglycine by Penicillin G acylase.
The parameters for complete hydrolysis of L-phenyl acetyl phenylglycine (L-PAPG) using immobilized penicillin G acylase (IMEPGA) were investigated. IMEPGA exhibited maximum activity at pH 8.5 and 50 degrees C. The apparent Km value observed was 10 mM. Quantitative hydrolysis (>97%) of the L-PAPG was achieved within 45 min, at pH 7.8 and 37 degrees C, when 0.5% (w/v) of DL-PAPG was used and the concentration of IMEPGA was 133 IU/gm of DL-PAPG. The IMEPGA was used for 50 cycles.
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