Compounds > p-hydroxyphenylglycine-methyl-ester

p-hydroxyphenylglycine-methyl-ester and phosphoric-acid

p-hydroxyphenylglycine-methyl-ester has been researched along with phosphoric-acid* in 1 studies

Other Studies

1 other study(ies) available for p-hydroxyphenylglycine-methyl-ester and phosphoric-acid

Article	Year
Enzymatic synthesis of amoxicillin via a one-pot enzymatic hydrolysis and condensation cascade process in the presence of organic co-solvents. Applied biochemistry and biotechnology, 2010, Volume: 160, Issue:7 A cascade reaction combining the enzymatic hydrolysis of Penicillin G potassium salt (PGK) with the kinetically controlled enzymatic coupling of in situ formed 6-aminopenicillanic acid (6-APA) with p-hydroxyphenylglycine methyl ester (D-HPGM) to give amoxicillin as the final product by using a single enzyme has been demonstrated successfully. Ethylene glycol (EG) was employed as a component of reaction buffer to improve the synthesis yield. Reaction parameters, including different cosolvents, EG content, the loading of immobilized penicillin G acylase (IPA), and reaction temperature and time were studied to evaluate their effects on the reaction. The best result of 55.2% yield was obtained from the reaction which was carried out in the mixed media containing 40% sodium dihydrogen phosphate buffer (apparent pH 6.0) and 60% EG (v/v), with the initial concentration 150 mM and 450 mM of PGK and D-HPGM, respectively, catalyzed by 50 IU/mL IPA at 25 degrees C for 10 h. The IPA could be recycled for nine batches without obviously losing of catalytic activity. The important strategy will have potential application in the beta-lactam antibiotics industry due to the advantages of saving the effort of isolating 6-APA, reducing usual enzymatic steps and the industrial cost of amoxicillin synthesis. Topics: Amoxicillin; Biocatalysis; Enzymes, Immobilized; Ethylene Glycol; Glycine; Hydrolysis; Penicillin Amidase; Penicillin G; Phosphoric Acids; Solvents; Temperature	2010

Article

Year

Enzymatic synthesis of amoxicillin via a one-pot enzymatic hydrolysis and condensation cascade process in the presence of organic co-solvents.

Applied biochemistry and biotechnology, 2010, Volume: 160, Issue:7

A cascade reaction combining the enzymatic hydrolysis of Penicillin G potassium salt (PGK) with the kinetically controlled enzymatic coupling of in situ formed 6-aminopenicillanic acid (6-APA) with p-hydroxyphenylglycine methyl ester (D-HPGM) to give amoxicillin as the final product by using a single enzyme has been demonstrated successfully. Ethylene glycol (EG) was employed as a component of reaction buffer to improve the synthesis yield. Reaction parameters, including different cosolvents, EG content, the loading of immobilized penicillin G acylase (IPA), and reaction temperature and time were studied to evaluate their effects on the reaction. The best result of 55.2% yield was obtained from the reaction which was carried out in the mixed media containing 40% sodium dihydrogen phosphate buffer (apparent pH 6.0) and 60% EG (v/v), with the initial concentration 150 mM and 450 mM of PGK and D-HPGM, respectively, catalyzed by 50 IU/mL IPA at 25 degrees C for 10 h. The IPA could be recycled for nine batches without obviously losing of catalytic activity. The important strategy will have potential application in the beta-lactam antibiotics industry due to the advantages of saving the effort of isolating 6-APA, reducing usual enzymatic steps and the industrial cost of amoxicillin synthesis.

Topics: Amoxicillin; Biocatalysis; Enzymes, Immobilized; Ethylene Glycol; Glycine; Hydrolysis; Penicillin Amidase; Penicillin G; Phosphoric Acids; Solvents; Temperature

2010