T
Timo Korpela
Researcher at University of Turku
Publications - 150
Citations - 2586
Timo Korpela is an academic researcher from University of Turku. The author has contributed to research in topics: Bacillus circulans & Cyclomaltodextrin glucanotransferase. The author has an hindex of 29, co-authored 150 publications receiving 2463 citations.
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Journal ArticleDOI
Microbial Dextran-Hydrolyzing Enzymes: Fundamentals and Applications
TL;DR: The major characteristics of these enzymes, the methods for analyzing their activities and biological roles, analysis of primary sequence data, and three-dimensional structures of dextranases have been dealt with in this review.
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Adhesive organelles of Gram‐negative pathogens assembled with the classical chaperone/usher machinery: structure and function from a clinical standpoint
TL;DR: This review summarizes current knowledge on the structure, function, assembly and biomedical applications of the superfamily of adhesive fimbrial organelles exposed on the surface of Gram-negative pathogens with the classical chaperone/usher machinery and reveals two functional families of the organells, respectively, possessing polyadhesive and monoadhesive binding.
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Colorimetric determination of β-cyclodextrin: two assay modifications based on molecular complexation of phenolphatalein
TL;DR: The decolorization of phenolphtalein upon complexation to cyclodextrins was studied to measure beta-cyclodextrin concentrations and the results were comparable to those obtained by HPLC analyses after prepurification of the samples.
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Effects of detergents on activity of microbial lipases as measured by the nitrophenyl alkanoate esters method
Pirkko Helistö,Timo Korpela +1 more
TL;DR: Eukaryotic and prokaryotic lipases roughly form two separate classes behaving quite differently in different detergents, with the high detergent tolerance of Bacillus sp.
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Functional attributes of the phosphate group binding cup of pyridoxal phosphate-dependent enzymes.
TL;DR: Twenty-four structures of pyridoxal-5'-phosphate (PLP)-dependent enzymes that represent five different folds are shown to share a common recognition pattern for the phosphate group of their PLP-ligands, known as the phosphate-binding cup, which provides a very stable anchoring point for PLP.