IMMOBILIZATION OF PENICILLIN-G ACYLASE ON FUNCTIONALIZED MACROPOROUS POLYMER BEADS

被引:33
作者
BAHULEKAR, RV
PRABHUNE, AA
SIVARAMAN, H
PONRATHNAM, S
机构
[1] NATL CHEM LAB,DIV CHEM ENGN,POONA 411008,MAHARASHTRA,INDIA
[2] NATL CHEM LAB,DIV BIOCHEM SCI,POONA 411008,MAHARASHTRA,INDIA
关键词
BIOCATALYST ENZYME IMMOBILIZATION; MACROPOROUS SUPPORT; POLYETHYLENEIMINE; PENICILLIN ACYLASE;
D O I
10.1016/0032-3861(93)90300-Y
中图分类号
O63 [高分子化学(高聚物)];
学科分类号
070305 ; 080501 ; 081704 ;
摘要
Macroporous beaded polymers of varying pore sizes were synthesized coated with polyethyleneimine and derivatized with glutaraldehyde to generate aldehyde pendant groups. Penicillin G acylase (EC 3.5.1.11) was immobilized by covalent binding and the performance of immobilized enzyme was evaluated in batch mode. The expression was estimated as 43%. The shift in pH optima was marginal. The optimum temperature shifted from 40 to 57-degrees-C and K(m) shifted from 31 to 12.8 mumol. Immobilization enhanced the thermal stability of the enzyme.
引用
收藏
页码:163 / 166
页数:4
相关论文
共 8 条
  • [1] POLYETHYLENEIMINE IN IMMOBILIZATION OF BIOCATALYSTS
    BAHULEKAR, R
    AYYANGAR, NR
    PONRATHNAM, S
    [J]. ENZYME AND MICROBIAL TECHNOLOGY, 1991, 13 (11) : 858 - 868
  • [2] KINETIC-BEHAVIOR OF IMMOBILIZED PENICILLIN ACYLASE
    CARLEYSMITH, SW
    DUNNILL, P
    LILLY, MD
    [J]. BIOTECHNOLOGY AND BIOENGINEERING, 1980, 22 (04) : 735 - 756
  • [3] STUDIES OF POROUS POLYMER GELS .2. STRUCTURE AND POROSITY OF MODERATELY CROSSLINKED POLY(METHACRYLIC ACID) GELS
    GALINA, H
    KOLARZ, BN
    [J]. JOURNAL OF APPLIED POLYMER SCIENCE, 1979, 24 (04) : 891 - 900
  • [4] KOILPILLAI L, 1990, J CHEM TECHNOL BIOT, V49, P173
  • [5] ADSORPTION AND EXPRESSION OF PENICILLIN-G ACYLASE IMMOBILIZED ONTO METHACRYLATE POLYMERS GENERATED WITH VARYING PORE GENERATING SOLVENT VOLUME
    KOTHA, A
    SELVARAJ, L
    RAJAN, CR
    PONRATHNAM, S
    KUMAR, KK
    AMBEKAR, GR
    SHEWALE, JG
    [J]. APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY, 1991, 30 (03) : 297 - 302
  • [6] LOWRY OH, 1951, J BIOL CHEM, V193, P265
  • [7] Mosbach R, 1976, Methods Enzymol, V44, P53
  • [8] SHEWALE JG, 1989, PROCESS BIOCHEM, V24, P146