| Autor: |
Ramirez, Hector L., Chico, Belkis, Villalonga Santana, Reynaldo, Houste, Katty, Schacht, Etienne H. |
| Předmět: |
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| Zdroj: |
Journal of Bioactive & Compatible Polymers; May2002, Vol. 17 Issue 3, p161, 12p |
| Abstrakt: |
Invertase from Saccharomyces cerevisiae was activated by periodate treatment and further reacted with ethylenediamine/sodium borohydride. Carboxymethylcellulose was then attached to ethylenediamine-modified invertase using l-ethyl-3-(3-dimethylaminopropyl) carbodiimide as coupling agent. The modified enzyme contained 3.5mol of polysaccharide per mol of holoenzyme, and retained about 56% of the initial invertase activity. The thermostability of invertase increased from 64 to 70°C, the thermal inactivation at different temperatures ranging from 60 to 70°C was markedly reduced for polymer-modified enzyme. An increase of 9.1 kJ mol[sup -1] in activation free energy of inactivation was determined for invertase after modification. Functional stability was increased for carboxymethylcellulose-invertase complex in the range of pH between 2.0 and 12.0. The conjugate was also more resistant to denaturation by 6 M urea solution. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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