Purification and Characterization of a Novel Prolyl Aminopeptidase fromMaitake(Grifola frondosa)

2004 ◽  
Vol 68 (6) ◽  
pp. 1395-1397 ◽  
Author(s):  
Kazuyuki HIWATASHI ◽  
Kazuyuki HORI ◽  
Keitaro TAKAHASHI ◽  
Akira KAGAYA ◽  
Shunzo INOUE ◽  
...  
Keyword(s):  
Grifola Frondosa ◽  
Purification And Characterization ◽  
Prolyl Aminopeptidase

Partial purification and characterization of Lys-N from Grifola frondosa using a novel, specific assay

2014 ◽  
Vol 3 (4) ◽  
pp. 275-281 ◽  
Author(s):  
Timo Stressler ◽  
Thomas Eisele ◽  
Ann-Kathrin Kleinthomä ◽  
Susanne Meyer ◽  
Lutz Fischer
Keyword(s):  
Grifola Frondosa ◽  
Partial Purification ◽  
Purification And Characterization ◽  
Specific Assay

scholarly journals Purification and characterization of β-N-acetylglucos-aminidase from Grifola frondosa

BioResources ◽  
2021 ◽  
Vol 16 (4) ◽  
pp. 7234-7248
Author(s):  
Yi-Cheng Wang ◽  
Te-Sheng Lien ◽  
Nan-Yin Chen ◽  
Tai-Hao Hsu
Keyword(s):  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Hydrolysis Product ◽  
Chitinase Activity ◽  
Grifola Frondosa ◽  
Purification And Characterization ◽  
Carbohydrate Utilization ◽  
Highly Active

Using commercial API-ZYM screening kits, highly active α-glucosidase, β-glucosidase, and β-N-acetylglucosaminidase were found in Grifola frondosa, having potential for carbohydrate utilization. Of these, β-N-acetylglucosaminidase, which converts chitin to N-acetylglucosamine, was purified and characterized. The recovery was 24.5%, and the purified enzyme had a specific activity 0.67 U/mg protein. Chitinase activity was confirmed by zymogram analysis. The enzyme was also shown to be β-N-acetylglucosaminidase, as N-acetylglucosamine was the main hydrolysis product from colloidal chitin. Thus, the molecule was named NAG38, to indicate β-N-acetylglucosaminidase activity and a molecular weight of 38 kDa, as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Enzymatic activity was optimal at pH 7.0 and 50 °C, with Km and Vmax values of 0.112 mM and 0.570 μmol/min/mg protein against p-nitrophenyl N-acetyl-β-D-glucosaminide. The bioactivity was inhibited by Hg2+, Ag+, Mg2+, Zn2+, Ca2+, and Mn2+, with residual enzyme bioactivity only 11.1% after incubation in Hg2+, but was not substantially inhibited by Ba2+, K+, and Na+.

Purification and characterization of phosphoglucomutase from peas

1994 ◽  
Vol 92 (3) ◽  
pp. 479-486 ◽  
Author(s):  
Cynthia M. Galloway ◽  
W. Mack Dugger
Keyword(s):  
Purification And Characterization
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