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ISSN 2410-7751 (Print)
ISSN 2410-776X (Online)

2 2016  

"Biotechnologia Acta" V. 9, No 2, 2016
Р.48-54 , Bibliography 13, English
Universal Decimal Classification: 577.158.54


O. V. Gudzenko, N. V. Borzova, L. D. Varbanets

Zabolotny Institute of Microbiology and Virology of the National Academy of Sciences of Ukraine, Kyiv

The aim of the research was a comparative study of the thermal stability of native and modified by various methods  α-L rhamnosidases of Eupenicillium erubescens and Cryptococcus albidus for improving the stability of enzymes. Denaturation of native and modified enzymes were performed at 65  0C, pH 5.2. Enzyme  activity  was  determined  using  p-nitrophenyl-α-L-rhamnopyranoside  and  naringin.  It  is  found that in the treatment by polyethylenglycol  PEG 1500, dextrans 500 and 70 T thermostability of  α-L-rhamnosidases  tested  decreases,  while  modification  with  polyethylenglycol    20000  leads  to  increase thermal stability of the E. erubescens enzyme to 280% and C. albidus to 150%. Comparative study of the thermal  stability  of  the  native  and  modified  by  cellulose  and  its  derivatives  α-L-rhamnosidases of  C.  albidus and  E.  erubescens showed  that  at  concentrations  cellulose  of  5–15 μg/10 μg  protein protective  effect  of  polymers  on  enzymes  was  investigated  was  observed.  Hydrophobic  modifications using  succinic  anhydride  also  can  slow  down  the  denaturation  of  α-L-rhamnosidases  tested  under experimental conditions. These stabilized C. albidus and E. erubescens α-L-rhamnosidases can be used in biotechnological processes.

Key words: α-L-rhamnosidase, Eupenicillium erubescens, Cryptococcus albidus, thermal stabilization of enzymes.

© Palladin Institute of Biochemistry of the National Academy of Sciences of Ukraine, 2016