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<span style="font-size:11.0pt;font-family: "Times New Roman";mso-fareast-font-family:"Times New Roman";mso-bidi-font-family: Mangal;mso-ansi-language:EN-GB;mso-fareast-language:EN-US;mso-bidi-language: HI" lang="EN-GB">A novel pullulanase from a fungus <i style="mso-bidi-font-style:normal">Hypocrea jecorina</i> QM9414: production and biochemical characterization</span>

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Title A novel pullulanase from a fungus Hypocrea jecorina QM9414: production and biochemical characterization
 
Creator Orhan, Nurdagul
Kiymaz, Nilay Altas
Peksel, Aysegul
 
Subject Hypocrea jecorina QM9414
Culture conditions
Induction
Type II pullulanase
Purification
 
Description 149-155
Pullulanase
production from a fungus Hypocrea jecorina QM9414 that produces native
extracellular hydrolases having industrial applications was carried out in a
shaking flask culture containing 0.5% amylopectin at a pH of 6.50 at 30°C.
The enzyme was purified 11-fold by ammonium sulfate fractionation,
anion-exchange and gel-filtration chromatographies with a yield of 10.12% and a
specific activity of 1.36 ± 0.14
U/mg protein. The molecular mass of pullulanase was estimated to be 130.56 kDa
by PAGE and SDS-PAGE, indicating that the native enzyme was a monomer. The
optimum pH and temperature for purified enzyme was 6.5 and between 35°-65°C, respectively. The Km
values for amylopectin, starch and
pullulan as substrates were 10.7, 15.5
and 38.4 mg/mL, respectively. The Vmax
values were found to be 3.32, 3.32 and 3.82 ΔA/min for amylopectin, starch and pullulan, respectively.
The enzyme was stable at 40-70°C for 30
min, but lost about 33% of its activity at 80°C and about 43% of activity at 90°C and 100°C for the
same incubation period. Pullulanase activity was stimulated by CoCl2,
NiCl2, KI, NaCl, MgCl2, and LiSO4. The enzyme
was slightly inhibited by urea, CaCl2 and
b-mercaptoethanol. The enyzmatic characteristics, substrate specificity
and the products of hydrolysis indicated that the enzyme was similar to those
of type II pullulanases.
 
Date 2014-04-30T07:01:12Z
2014-04-30T07:01:12Z
2014-04
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/28693
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.51(2) [April 2014]