Kristiina Kruus

ORCID: 0000-0003-4749-264X
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About
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Research Areas
  • Biofuel production and bioconversion
  • Enzyme-mediated dye degradation
  • Microbial Metabolism and Applications
  • Advanced Cellulose Research Studies
  • melanin and skin pigmentation
  • Lignin and Wood Chemistry
  • Enzyme Production and Characterization
  • Biochemical and biochemical processes
  • Microbial Metabolic Engineering and Bioproduction
  • Polysaccharides and Plant Cell Walls
  • Catalysis for Biomass Conversion
  • Fermentation and Sensory Analysis
  • Enzyme Catalysis and Immobilization
  • Food composition and properties
  • biodegradable polymer synthesis and properties
  • Dyeing and Modifying Textile Fibers
  • Proteins in Food Systems
  • Biochemical Analysis and Sensing Techniques
  • Dye analysis and toxicity
  • Phytochemicals and Antioxidant Activities
  • Metal-Catalyzed Oxygenation Mechanisms
  • Meat and Animal Product Quality
  • Analytical chemistry methods development
  • Protein Hydrolysis and Bioactive Peptides
  • Polyamine Metabolism and Applications

VTT Technical Research Centre of Finland
2014-2024

Aalto University
2020-2024

Tieto (Finland)
2001-2024

Synthetic Biologics (United States)
2018

Kookmin University
2018

Espoo Music Institute
2016

Bioengineering Center
2014

National Center for Genetic Engineering and Biotechnology
2014

John Wiley & Sons (United States)
2014

University of Helsinki
2005-2010

Lignin-derived inhibition is a major obstacle restricting the enzymatic hydrolysis of cell wall polysaccharides especially with softwood lignocellulosics. Enzyme adsorption on lignin suggested to contribute inhibitory effect lignin. The interaction cellulases was studied in present work commercial Trichoderma reesei (Celluclast) and lignin-rich residues isolated from steam pretreated (SPS) by acid hydrolysis. Both preparations inhibited microcrystalline cellulose (Avicel) adsorbed cellulase...

10.1002/bit.23242 article EN Biotechnology and Bioengineering 2011-06-23

To discover novel laccases potential for industrial applications.Fungi were cultivated on solid media containing indicator compounds that enabled the detection of as specific colour reactions. The indicators used Remazol Brilliant Blue R (RBBR), Poly R-478, guaiacol and tannic acid. screening work resulted in isolation 26 positive fungal strains. Liquid cultivations strains confirmed four efficient laccase producers found screening. Biochemical characteristics typical terms molecular weight,...

10.1111/j.1365-2672.2004.02348.x article EN Journal of Applied Microbiology 2004-07-28

Previous studies on Melanocarpus albomyces laccase have shown that this enzyme is very interesting for both basic research purposes and industrial applications. In order to obtain a reliable efficient source laccase, it was produced in the filamentous fungus Trichoderma reesei . Two approaches were used: production of non-fused hydrophobin–laccase fusion protein. Both proteins expressed T. under cbh1 promoter, significantly higher activities obtained with shake-flask cultures (corresponding...

10.1099/mic.0.27147-0 article EN Microbiology 2004-09-01

Laccase‐catalyzed polymerization of tyrosine and tyrosine‐containing peptides was studied in the presence absence ferulic acid (FA). Advanced spectroscopic methods such as MALDI‐TOF MS, EPR, FTIR microscopy HPLC‐fluorescence, well more conventional analytical tools: oxygen consumption measurements SDS/PAGE were used reaction mechanism studies. Laccase found to oxidize peptides, with consequent compounds. The covalent linkage connecting compounds be an ether bond. Only small amounts...

10.1111/j.1742-4658.2005.04786.x article EN FEBS Journal 2005-07-01

Cross-linking enzymes generate covalent bonds in and between food biopolymers. These are interesting tools for tailoring dough bread structures, as the characteristics of biopolymers significantly determine viscoelastic fracture properties bread. In this study, influence oxidative cross-linking enzymes, tyrosinase from filamentous fungus Trichoderma reesei laccase white rot Trametes hirsuta, on were examined. Oxidation low molecular weight phenolic model compounds flour, gluten proteins,...

10.1021/jf0703349 article EN Journal of Agricultural and Food Chemistry 2007-06-28

A homology search of the genome database filamentous fungus Trichoderma reesei identified a new T. tyrosinase gene tyr2 , encoding protein with putative signal sequence. The was overexpressed in native host under strong cbh1 promoter, and enzyme secreted into culture supernatant. This is first report on fungal tyrosinase. Expression TYR2 resulted good yields, corresponding to approximately 0.3 1 g·L −1 shake flask cultures laboratory‐scale batch fermentation, respectively. purified...

10.1111/j.1742-4658.2006.05429.x article EN FEBS Journal 2006-08-29

Tyrosinase production by Pycnoporus cinnabarinus and sanguineus was screened among 20 strains originating from various geographical areas, particularly tropical environments. The tyrosinase the most efficient strain purified characterized tested for food additive applications.Monophenolase diphenolase activities of were measured cell lysate strains, 8-10 days cultivation. P. CBS 614.73 showed highest productivity (45.4 163.6 U g(-1) protein per day monophenolase respectively). concentrated...

10.1111/j.1365-2672.2004.02481.x article EN Journal of Applied Microbiology 2005-01-19

Understanding the enzymatic hydrolysis of cellulose and influence lignin in process are critical for viable production fuels chemicals from lignocellulosic biomass. The interactions monocomponent cellulases with substrates were investigated by using thin films supported on quartz crystal microgravimetry (QCM) resonators. Trichoderma reesei exoglucanase (CBH-I) endoglucanase (EG-I) bound strongly to both but EG-I exhibited a distinctive higher affinity lignin, causing more extensive...

10.1021/bm400230s article EN Biomacromolecules 2013-03-13

The use of [EMIM]AcO and three DESs was compared in lignocellulose pretreatment with focus on cellulase stability, effects enzymatic hydrolysis pretreated both buffer solutions ionic liquid or DES.

10.1039/c6ra11719h article EN RSC Advances 2016-01-01
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