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Effect of ionic liquids on the structure, stability and activity of two related α-amylases

被引：57
作者：
Dabirmanesh, Bahareh [1 ]
Daneshjou, Sara [2 ]
Sepahi, Abbas Akhavan [3 ]
Ranjbar, Bijan [4 ]
Khavari-Nejad, Ramazan Ali [2 ]
Gill, Pooria [5 ]
Heydari, Akbar [6 ]
Khajeh, Khosro [1 ]
机构：
[1] Tarbiat Modares Univ, Dept Biochem, Fac Biol Sci, Tehran, Iran
[2] Islamic Azad Univ, Dept Microbiol, Fac Sci, Sci & Res Branch, Tehran, Iran
[3] Islamic Azad Univ, Dept Microbiol, Fac Sci, North Branch, Tehran, Iran
[4] Tarbiat Modares Univ, Dept Biophys, Fac Biol Sci, Tehran, Iran
[5] Tarbiat Modares Univ, Dept Nanobiotechnol, Fac Biol Sci, Tehran, Iran
[6] Tarbiat Modares Univ, Dept Chem, Fac Sci, Tehran, Iran
来源：
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES | 2011年 / 48卷 / 01期
关键词：
alpha-Amylase; Ionic liquids; Differential scanning calorimetry (DSC); Fluorescence spectroscopy; Stability; ANTARCTICA LIPASE-B; AQUEOUS-SOLUTIONS; BIOCATALYSIS; DISSOLUTION; SOLVENTS; PROTEIN; STARCH; MEDIA;
D O I：
10.1016/j.ijbiomac.2010.10.001
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
070307 [化学生物学]; 071010 [生物化学与分子生物学];
摘要：
Ionic liquids are recognized as green solvents for carbohydrates dissolution. However, only a limited number of studies have been carried out to investigate their effect on carbohydrate hydrolyzing enzymes. We have investigated the influence of two water miscible ionic liquids on the activity, stability and structure of two related alpha-amylases from Bacillus amyloliquefaciens and Bacillus lichiniformis. Upon changes in ionic liquids concentrations, both enzymes activity and stability were reduced. Associated thermodynamic and conformational changes were observed using differential scanning calorimetry and fluorescence techniques. Thermal denaturation was accompanied by aggregation in both aqueous buffer and [BMIm][Cl) but [HMIm][Cl] significantly suppressed aggregation. (C) 2010 Elsevier B.V. All rights reserved.
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页码：93 / 97
页数：5
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