Characterization of glucose oxidase from Penicillium notatum
Summary: In the present study glucose oxidase (GOD) has been isolated from a culture filtrate of Penicillium notatum. The enzyme was purified by ammonium sulphate precipitation, diethylaminoethyl (DEAE) cellulose ion-exchange chromatography and Sephadex gel filtration. This protocol gave 16.47-fold...
| Permalink: | http://skupnikatalog.nsk.hr/Record/nsk.NSK01000736154/Details |
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| Matična publikacija: |
Food technology and biotechnology 47 (2009), 3 ; str. 331-335 |
| Glavni autor: | Nawaz Bhatti, Haq (-) |
| Ostali autori: | Saleem, Nabeela (-) |
| Vrsta građe: | Članak |
| Jezik: | eng |
| Predmet: | |
| Online pristup: |
Food Technology and Biotechnology |
| LEADER | 01923caa a2200289 ir4500 | ||
|---|---|---|---|
| 001 | NSK01000736154 | ||
| 003 | HR-ZaNSK | ||
| 005 | 20121012100031.0 | ||
| 007 | ta | ||
| 008 | 100510s2009 ci ||| ||eng | ||
| 035 | |9 (HR-ZaNSK)738778 | ||
| 035 | |a (HR-ZaNSK)000736154 | ||
| 040 | |a HR-ZaNSK |b hrv |c HR-ZaNSK |e ppiak | ||
| 042 | |a croatica | ||
| 080 | |a 57 |2 MRF 1998. | ||
| 100 | 1 | |a Nawaz Bhatti, Haq | |
| 245 | 1 | 0 | |a Characterization of glucose oxidase from Penicillium notatum / |c Haq Nawaz Bhatti and Nabeela Saleem. |
| 300 | |b Ilustr. | ||
| 500 | |a Congress of Croatian society of biochemistry and molecular biology, Osijek, Croatia, 17-20 September 2008 | ||
| 504 | |a Bibliografija: 24 jed | ||
| 520 | 8 | |a Summary: In the present study glucose oxidase (GOD) has been isolated from a culture filtrate of Penicillium notatum. The enzyme was purified by ammonium sulphate precipitation, diethylaminoethyl (DEAE) cellulose ion-exchange chromatography and Sephadex gel filtration. This protocol gave 16.47-fold purification and 25 % recovery of the enzyme. The optimum pH and temperature for the activity were 5.4 and 45 °C, respectively. The Km and vmax values for the enzyme were 10.5 mM and 456 U/mg, respectively. A detailed kinetic study of thermal inactivation was carried out. Both enthalpy of activation (ΔH*) and entropy of activation (ΔS*) decreased at higher temperatures. Moreover, free energy of denaturation (ΔG*) increased at higher temperature, making the enzyme thermally stable. A possible explanation for the thermal inactivation of GOD at higher temperatures is also discussed | |
| 653 | 0 | |a Penicillium notatum |a Glukoza-oksidaza | |
| 700 | 1 | |a Saleem, Nabeela | |
| 773 | 0 | |t Food technology and biotechnology |x 1330-9862 |g 47 (2009), 3 ; str. 331-335 |w nsk.(HR-ZaNSK)000174173 | |
| 981 | |b B03/09 | ||
| 998 | |a Luko100510 |c vol2o121012 | ||
| 856 | 4 | 2 | |u http://hrcak.srce.hr/ftb |y Food Technology and Biotechnology |