Decolorization of Azo, Triphenyl Methane, Heterocyclic, and Polymeric Dyes by Lignin Peroxidase Isoenzymes from Phanerochaete chrysosporium
- P. Ollikka, Kirsi Alhonmäki, V. Leppänen, T. Glumoff, Timo Raijola, I. Suominen
- Biology, ChemistryApplied and Environmental Microbiology
- 1 December 1993
The ligninolytic enzyme system of Phanerochaete chrysosporium decolorizes several recalcitrant dyes and the ability of the isoenzymes to decolorize the dyes in the presence of veratryl alcohol was generally comparable to that of the crude enzyme preparation, suggesting that lignin peroxidase plays a major role in the decolorization.
The Os and Nd isotopic systematics of c. 2.44 Ga Akanvaara and Koitelainen mafic layered intrusions in northern Finland
- E. Hanski, R. Walker, H. Huhma, I. Suominen
- Geology
- 15 June 2001
C-terminal truncations of a thermostable Bacillus stearothermophilus alpha-amylase.
- M. Vihinen, T. Peltonen, A. Iitiä, I. Suominen, P. Mäntsälä
- Biology, ChemistryProtein Engineering
- 1 October 1994
The mutations introducing new translation termination sites shortened the 515 amino acid residue-long wild type enzyme by 17, 32, 47, 73 or 93 residues, and the consequences of the truncation to the structure and function of the enzymes were explored with molecular modeling.
Expression in Pichia pastoris and purification of Aspergillus awamori glucoamylase catalytic domain.
- H. Heimo, K. Palmu, I. Suominen
- BiologyProtein Expression and Purification
- 1997
The expression in Pichia pastoris, purification, and characterization of the Aspergillus awamori glucoamylase catalytical domain (GAc) are reported and GAc, a glycoprotein heterologously expressed in P. pastoris is N- and O-glycosylated, with 23% carbohydrate content.
Fusion tails for the recovery and purification of recombinant proteins.
- C. Ford, I. Suominen, C. Glatz
- BiologyProtein Expression and Purification
- 1 April 1991
Site-directed mutagenesis of a thermostable alpha-amylase from Bacillus stearothermophilus: putative role of three conserved residues.
- M. Vihinen, P. Ollikka, P. Mäntsälä
- BiologyJournal of Biochemistry (Tokyo)
- 1 February 1990
This mutant enzyme had a wider pH range but about the same temperature optimum and thermal stability as the wild-type enzyme, and in prolonged incubation this mutant enzyme showed an altered end-product profile by liberating only maltose and maltotriose.
Recovery of a charged‐fusion protein from cell extracts by polyelectrolyte precipitation
- D. Parker, C. Glatz, C. Ford, S. Gendel, I. Suominen, M. Rougvie
- BiologyBiotechnology and Bioengineering
- 20 August 1990
β‐Galactosidase served as a model system to explore the feasibility of enhancing the selectivity of a low‐cost, easily scaled separation method—precipitation. Enhanced selectivity was sought by…
Extracellular production of cloned α-amylase by Escherichia coli
- I. Suominen, M. Karp, P. Mäntsälä
- Biology
- 1987
Expression in Pichia pastorisand Purification of Aspergillus awamoriGlucoamylase Catalytic Domain
- H. Heimo, K. Palmu, I. Suominen
- Biology
- 1 June 1997
Pichia pastoris produced GAc to the level of 0.4 g per liter medium, which is about the same level as that gained for recombinant GA from Aspergillus and about 100-fold more than previously achieved by Saccharomyces cerevisiae.
Effects of signal peptide mutations on processing of Bacillus stearothermophilus alpha-amylase in Escherichia coli.
- I. Suominen, P. Meyer, P. Mäntsälä
- BiologyMicrobiology
- 1 March 1995
Processing of the signal peptide was remarkably tolerant to mutations, because switching between the alternative sites was possible and some mutations more distal to the cleavage site also affected the site preference.
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