Biomedical Engineering Reference
In-Depth Information
Chapter 5
O
BTAINING AND
P
ROPERTIES OF
I
NTRACELLULAR
A
MINOACYLASE
E
SCHERICHIA
C
OLI
H. S. Yepremyan
*
«BIO-CHIM» Ltd., Yerevan, Armenia
A
BSTRACT
Isolation and purification method of intracellular aminoacylase
Escherichia coli
with
use of ion-exchange chromatography on DEAE cellulose is developed. Ferment is
obtained with 30% yield activity and 32-fold purified. Physico-chemical properties of
investigating ferment is studied.
Keywords:
L-aminoacylase, intracellular ferment, Escherichia coli, chromatography,
properties
Aminoacylase (N-acylamino acid amidohydrolase, EC 3.5.1.14) hydrolyzes amide bonds
of N-acylated amino acids. This ferment is found in different microorganisms, animals and
other objects. The aminoacylase in native as well as in immobilized state is used in industrial
scales for production of optically active amino acids. Widely practical application of
stereoselective hydrolysis of acylated amino acids became possible due to researches of
Greenstein et al. [1], who managed to isolate from racemates practically from all native and
some synthetic amino acids with use of homogenate of pig kidney or partially purified
preparation acylase I of pig kidney. More detailed investigations of the process of obtaining
and study of aminoacylase were performed by Japanese scientists, who used ferment from
Aspergillus oryzae
[2-4] for this purpose. Now there are a lot of articles devoted to obtaining
and investigation of properties of different aminoacylase preparations, isolated from different
microorganisms:
M. agilis
[5],
Str. olivoreticuli
[6],
Asp. oryzae
[7]. However as opposed to
comparatively well studied extracellular aminoacylases, intracellular aminoacylases are not
enough characterized. For this reason the study of intracellular aminoacylase is pressing issue.
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