Zobrazeno 1 - 10
of 26
pro vyhledávání: '"Sawraj Singh"'
Publikováno v:
Microbial Products ISBN: 9781003306931
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::99f293a53ee9763e8fa066676daf6b93
https://doi.org/10.1201/9781003306931-4
https://doi.org/10.1201/9781003306931-4
Publikováno v:
India -- West; 3/7/2014, Vol. 39 Issue 16, pB16-B16, 1/8p
Publikováno v:
Bioresource Technology. 99:2116-2120
Lipases of a newly isolated Pseduomonas aeruginosa MTCC 5113 were assessed for transesterification of benzyl alcohol and vinyl acetate to produce the flavoring agent benzyl acetate. Crude lipase preparations that minimized the cost of the biocatalyst
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::75d731ac070542dfbfbefbf3337f10e4
https://doi.org/10.1016/j.biortech.2007.05.041
https://doi.org/10.1016/j.biortech.2007.05.041
Autor:
Uttam Chand Banerjee, Sawraj Singh
Publikováno v:
Process Biochemistry. 42:1063-1068
Enantiospecific lipase was purified from Pseudomonas aeruginosa MTCC 5113 and it was used for the hydrolysis of (±)-methyl trans -3(4-methoxyphenyl) glycidate, a key intermediate in the synthesis of cardiovascular drug, diltiazem. Enzyme from broth
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::54d277b125fbf6c0695165c2f50c94f9
https://doi.org/10.1016/j.procbio.2007.04.006
https://doi.org/10.1016/j.procbio.2007.04.006
Publikováno v:
Bioprocess and Biosystems Engineering. 28:341-348
A lipase producing bacterium has been isolated from the soil to enantiospecifically hydrolyze the (+/-)-methyl trans-3(4-methoxyphenyl) glycidate (MPGM), an intermediate in the synthesis of cardiovascular drug, diltiazem. This hydrolysis provided the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c44b20268b6ce8035b1c286559dbec2a
https://doi.org/10.1007/s00449-005-0039-7
https://doi.org/10.1007/s00449-005-0039-7
Autor:
Sawraj Singh, Uttam Chand Banerjee
Publikováno v:
Journal of Molecular Catalysis B: Enzymatic. 36:30-35
A potent bacterial strain, Pseudomonas aeruginosa, has been isolated from the soil which produces extracellular lipase that can carry out the excellent stereospecific hydrolysis of trans-3-(4-methoxyphenyl)glycidic acid methyl ester [(±)-MPGM)] to g
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0922e1bad9ddd692261a2bfc1254b86c
https://doi.org/10.1016/j.molcatb.2005.07.005
https://doi.org/10.1016/j.molcatb.2005.07.005
Publikováno v:
Talanta. 75(1)
Sensitive and specific, high-performance liquid chromatography (HPLC) methods have been developed and validated for linearity, accuracy and precision for the quantification of dl-3-phenyllactic acid, dl-O-acetyl-3-phenyllactic acid and (+/-)-mexileti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::66d876672dbe3da8b51edcaaf4475cf0
https://pubmed.ncbi.nlm.nih.gov/18371874
https://pubmed.ncbi.nlm.nih.gov/18371874
Publikováno v:
Bioprocess & Biosystems Engineering; Apr2006, Vol. 28 Issue 5, p341-348, 8p
Autor:
Karen Holt-Tiffin, Sateesh Deshaboina, Hare Krishnen, Rakeshwar Bandichhor, Richard Lloyd, Manpreet Singh, Sawraj Singh, Apurba Bhattacharya
Publikováno v:
Catalysis Science & Technology. 2:1602
A whole-cell mediated asymmetric reduction of oxcarbazepine 1 to S-licarbazepine 2, a key intermediate in the synthesis of Eslicarbazepine acetate, was achieved using the yeast strain Pichia methanolica 103660. The reduction was carried out in a biph
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bc20f2f9bc576bdbd6a124bdf54ad9a1
https://doi.org/10.1039/c2cy00537a
https://doi.org/10.1039/c2cy00537a
Publikováno v:
Bioresource Technology. 100:1884
Biocatalysis Laboratory, Department of Pharmaceutical Technology (Biotechnology), National Institute of Pharmaceutical Education and Research, Sector 67, S.A.S. Nagar 160 062, India Carbohydrate and Protein Laboratory, Department of Biotechnology, Pu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0a234a53dfa7a4e8086ae197ec73f7dc
https://doi.org/10.1016/j.biortech.2008.09.038
https://doi.org/10.1016/j.biortech.2008.09.038