Isolation and properties of recombinant inulinases from Aspergillus sp.
The genes inuA and inu1, encoding two inulinases (32nd glycosyl hydrolase family) from filamentous fungi Aspergillus niger and A. awamori, were cloned into Penicillium canescens recombinant strain. Using chromatographic techniques, endoinulinase InuA (56 kDa, pI 3) and exoinulinase Inu1 (60 kDa, pI 4.3) were purified to homogeneity from the enzymatic complexes of P. canescens new transformants. The properties, such as substrate specificity, pH- and T-optima of activity, stability at different temperatures, influence of cations and anions on the catalytic activity, etc., of both recombinant inulinases were studied.
Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky pr. 33/2, 119071 Moscow, Russia.
P V
PV
Volkov
O A
OA
Sinitsyna
E A
EA
Fedorova
A M
AM
Rojkova
A D
AD
Satrutdinov
I N
IN
Zorov
O N
ON
Okunev
A V
AV
Gusakov
A P
AP
Sinitsyn
D001230:Aspergillus / Q000201:enzymology*; D005656:Fungal Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D006026:Glycoside Hydrolases / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010407:Penicillium / Q000378:metabolism; D055550:Protein Stability; D011994:Recombinant Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D013379:Substrate Specificity; D013696:Temperature
D005656:Fungal Proteins; D011994:Recombinant Proteins; D006026:Glycoside Hydrolases; C023086:inulinase