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STABILITY OF NATIVE AND MODIFIED α-GALACTOSIDASE OF Cladosporium cladosporioides
Ukrainian Biochemical Journal
|November 10, 2015
Summary
Modifying the carbohydrate component of alpha-galactosidase (α-galactosidase) with sodium periodate significantly reduced its activity and altered its thermal stability. This suggests carbohydrate structure is crucial for enzyme function.
Area of Science:
- Biochemistry
- Enzymology
- Glycobiology
Background:
- Glycoproteins' carbohydrate components play vital roles in protein structure and function.
- Understanding these roles is key to enzyme engineering and application.
Purpose of the Study:
- To investigate the impact of modifying the carbohydrate moiety of Cladosporium cladosporioides α-galactosidase using sodium periodate oxidation.
- To compare the activity and stability of native and modified α-galactosidase.
Main Methods:
- Enzyme activity assays using synthetic (n-nitrophenyl) and natural substrates (melibiose, raffinose, stachyose).
- Assessment of thermal stability across a temperature range (20-60 °C).
- Evaluation of residual activity after exposure to various alcohol concentrations (methanol, ethanol, propanol).
Main Results:
- Sodium periodate modification significantly decreased α-galactosidase activity and affinity for substrates.
- The optimal temperature range for the modified enzyme shifted to lower temperatures (30-50 °C) compared to the native enzyme (20-60 °C).
- Modified α-galactosidase exhibited altered stability in organic solvents and higher thermal stability under neutral pH.
Conclusions:
- Modification of the carbohydrate component critically affects α-galactosidase catalytic properties.
- Observed changes in activity and stability are likely due to alterations in the enzyme's tertiary and quaternary protein structure.
