A green, fully enzymatic procedure for amine resolution, using a lipase and a penicillin G acylase

被引：23
作者：
Ismail, Hilda [1 ]
Lau, Rute Madeira [1 ]
van Langen, Luuk M. [1 ]
van Rantwijk, Fred [1 ]
Svedas, Vytas K. [2 ,3 ]
Sheldon, Roger A. [1 ]
机构：
[1] Delft Univ Technol, Dept Biotechnol, Lab Biocatalysis & Organ Chem, NL-2628 BL Delft, Netherlands
[2] Moscow MV Lomonosov State Univ, Fac Bioengn & Bioinformat, Moscow 119992, Russia
[3] Moscow MV Lomonosov State Univ, Belozersky Inst Physicochem Biol, Moscow 119992, Russia
来源：
GREEN CHEMISTRY | 2008年 / 10卷 / 04期
关键词：
D O I：
10.1039/b714088f
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
A green procedure for the kinetic resolution of chiral amines via enzymatic acylation and deacylation has been demonstrated. The fully enzymatic approach obviates the common, waste-generating deacylation under strongly alkaline conditions. The acylating agent was (R)-phenylglycine propyl ester in combination with Candida antarctica lipase B as acylation catalyst. The enantiomerically enriched amides were subsequently deacylated in the presence of the penicillin G acylase from Alcaligenes faecalis. The degree of enantiomer recognition by CaLB in the acylation of aliphatic amines was unexpectedly modest, but a considerable further enantiomeric enrichment could be accomplished in the course of the subsequent enzymatic hydrolysis step.
引用
收藏
页码：415 / 418
页数：4
相关论文
共 20 条
  • [1] Optically active amines via lipase-catalyzed methoxyacetylation
    Balkenhohl, F
    Ditrich, K
    Hauer, B
    Ladner, W
    [J]. JOURNAL FUR PRAKTISCHE CHEMIE-CHEMIKER-ZEITUNG, 1997, 339 (04): : 381 - 384
  • [2] Structural and energetic determinants for enantiopreferences in kinetic resolution of lipases
    Bocola, M
    Stubbs, MT
    Sotriffer, C
    Hauer, B
    Friedrich, T
    Dittrich, K
    Klebe, G
    [J]. PROTEIN ENGINEERING, 2003, 16 (05): : 319 - 322
  • [3] Molecular basis for the enhanced lipase-catalyzed N-acylation of 1-phenylethanamine with methoxyacetate
    Cammenberg, Maria
    Hult, Karl
    Park, Seongsoon
    [J]. CHEMBIOCHEM, 2006, 7 (11) : 1745 - 1749
  • [4] Bioreactor cultivation of Escherichia coli for production of recombinant penicillin G amidase from Alcaligenes faecalis
    Deak, PM
    Lutz-Wahl, S
    Bothe, H
    Fischer, L
    [J]. BIOTECHNOLOGY LETTERS, 2003, 25 (05) : 397 - 400
  • [5] DEZOETE MC, 1995, RECL TRAV CHIM PAY B, V114, P171
  • [6] An 'easy-on, easy-off' protecting group for the enzymatic resolution of (±)-1-phenylethylamine in an aqueous medium
    Guranda, DT
    Khimiuk, AI
    van Langen, LM
    van Rantwijk, F
    Sheldon, RA
    Svedas, VK
    [J]. TETRAHEDRON-ASYMMETRY, 2004, 15 (18) : 2901 - 2906
  • [7] Highly efficient and enantioselective enzymatic acylation of amines in aqueous medium
    Guranda, DT
    van Langen, LM
    van Rantwijk, F
    Sheldon, RA
    Svedas, VK
    [J]. TETRAHEDRON-ASYMMETRY, 2001, 12 (11) : 1645 - 1650
  • [8] Hieber G, 2001, CHIM OGGI, V19, P16
  • [9] Proteolytic processing of penicillin amidase from Alcaligenes faecalis cloned in E-coli yields several active forms
    Ignatova, Z
    Stoeva, S
    Galunsky, B
    Hörnle, C
    Nurk, A
    Piotraschke, E
    Voelter, W
    Kasche, V
    [J]. BIOTECHNOLOGY LETTERS, 1998, 20 (10) : 977 - 982
  • [10] PRODUCTS OF ACYLASE AND BETA-LACTAMASE HYDROLYSIS OF SOME PENICILLINS
    KULHANEK, M
    TADRA, M
    [J]. FOLIA MICROBIOLOGICA, 1968, 13 (04) : 340 - &
12