Table of Contents
ISRN Biotechnology
Volume 2013, Article ID 737805, 7 pages
Research Article

Macromolecular Crowding Enhances Catalytic Efficiency and Stability of α-Amylase

1Department of Protein Chemistry and Technology, Central Food Technological Research Institute, Mysore 570 020, India
2Max-Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, 06120 Halle (Saale), Germany

Received 20 June 2012; Accepted 13 August 2012

Academic Editors: E. Formentin and J. Sereikaite

Copyright © 2013 Jay Kant Yadav. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


In the present study an attempt was made to investigate the macromolecular crowding effect on functional attributes of α-amylase. High concentrations of sugar based cosolvents, (e.g., trehalose, sucrose, sorbitol, and glycerol) were used to mimic the macromolecular crowding environment (of cellular milieu) under in vitro conditions. To assess the effect of macromolecular crowding, the activity and structural properties of the enzyme were evaluated in the presence of different concentrations of the above cosolvents. Based on the results it is suggested that the macromolecular crowding significantly improves the catalytic efficiency of the enzyme with marginal change in the structure. Out of four cosolvents examined, trehalose was found to be the most effective in consistently enhancing thermal stability of the enzyme. Moreover, the relative effectiveness of the above cosolvents was found to be dependent on their concentration used.