Purification, Properties and Structural Aspects of a Thermoacidophilic alpha-Amylase from Alicyclobacillus Acidocaldarius Atcc 27009. Insight into Acidostability of Proteins-Reference-Cited by-同舟云学术

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Purification, Properties and Structural Aspects of a Thermoacidophilic alpha-Amylase from Alicyclobacillus Acidocaldarius Atcc 27009. Insight into Acidostability of Proteins

Published:1994-12 Issue:3 Volume:226 Page:981-991
ISSN:0014-2956
Container-title:European Journal of Biochemistry
language:en
Short-container-title:Eur J Biochem

Author:

Schwermann Birgit,Pfau Karsten,Liliensiek Birgit,Schleyer Manfred,Fischer Thomas,Bakker Evert P.

Publisher

Wiley

Subject

Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1994.00981.x/fullpdf

Reference66 articles.

1. Protein stability and molecular adaptation to extreme conditons

2. Proline residues responsible for thermostability occur with high frequency in the loop regions of an extremely thermostable oligo-1,6-glucosidase from Bacillus thermoglucosidasius KP1006.

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