Invertase from hyper producer strain of Aspergillus niger: physiochemical properties, thermodynamics and active site residues heat of ionization.
Here we report for the first time heat of ionization of invertase (E.C.3.2.1.26) active site residues from hyper-producer strain of Aspergillus niger (34.1 U ml(-1)), along with its physiochemical properties, kinetics and thermodynamics of stability-function. The Invertase showed great potential for industry as being highly efficient (k(cat) = 24167 s(-1) at 65 degrees C, pH 5.0) and stable (half life= 12 h at 56 degrees C).
Nadeem
Habibullah
H
Enzyme Engineering Lab., National Institute for Biotechnology and Genetic Engineering (NIBGE), P.O. Box 577, Jhang Road, Faisalabad, Pakistan.
Rashid
Muhammad Hamid
MH
Riaz
Muhammad
M
Asma
Bibi
B
Javed
Muhammad Rizwan
MR
Perveen
Raheela
R
D001234:Aspergillus niger / Q000201:enzymology* / Q000235:genetics; D020134:Catalytic Domain; D055598:Chemical Phenomena; D004795:Enzyme Stability; D007700:Kinetics; D013696:Temperature; D013816:Thermodynamics; D043324:beta-Fructofuranosidase / Q000737:chemistry* / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism
D043324:beta-Fructofuranosidase