M. Ângela Taipa

ORCID: 0000-0003-3776-180X
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About
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Research Areas
  • Protein purification and stability
  • Enzyme Catalysis and Immobilization
  • Monoclonal and Polyclonal Antibodies Research
  • Click Chemistry and Applications
  • Glycosylation and Glycoproteins Research
  • Transgenic Plants and Applications
  • Microbial Metabolic Engineering and Bioproduction
  • Viral Infectious Diseases and Gene Expression in Insects
  • Microbial Metabolism and Applications
  • Chemical Synthesis and Analysis
  • Protein Structure and Dynamics
  • Protein Interaction Studies and Fluorescence Analysis
  • Analytical Chemistry and Chromatography
  • Polymer Surface Interaction Studies
  • Bacterial Genetics and Biotechnology
  • Advanced Biosensing Techniques and Applications
  • Surfactants and Colloidal Systems
  • Effects and risks of endocrine disrupting chemicals
  • Microplastics and Plastic Pollution
  • Algal biology and biofuel production
  • Fermentation and Sensory Analysis
  • RNA and protein synthesis mechanisms
  • Hydrogels: synthesis, properties, applications
  • biodegradable polymer synthesis and properties
  • RNA modifications and cancer

Instituto Superior Técnico
2000-2024

Institute for Biotechnology and Bioengineering
2007-2024

University of Lisbon
2002-2023

Instituto Politécnico de Lisboa
1992-2013

Instituto de Biologia Experimental e Tecnológica
1993-2006

Rational design and combinatorial chemistry were utilized to search for lead protein L (PpL) mimetics application as affinity ligands the purification of antibodies small fragments, such Fab scFv, potential diagnostic or therapeutic agents. Inspection key structural features complex between PpL human prompted de novo synthesis a 169-membered solid-phase ligand library, which was assessed binding IgG subsequent selectivity fragment. Eight selected, chemically characterized compared with...

10.1002/jmr.733 article EN Journal of Molecular Recognition 2005-01-01

Phosphorus-31 nuclear magnetic resonance ((31)P NMR) was used to compare the anaerobic metabolism of glucose by suspended and gel-entrapped Saccharomyces bayanus cells. The fermentation carried out in a reaction system with continuous circulation through NMR sample tube. intracellular pH levels some phosphorylated compounds were noninvasively monitored (31)P while glucose, products, biomass determined analytic techniques comparisons showed that no significant differences are observed...

10.1002/bit.260410607 article EN Biotechnology and Bioengineering 1993-03-15

Abstract Chitin is the most abundant natural polymer in oceans, where it primarily recycled by chitin-degrading microorganisms. Endozoicomonadaceae (Oceanospirillales) bacteria are prominent symbionts of sessile marine animals, particularly corals, and presumably contribute to nutrient cycling their hosts. To reveal chitinolytic potential this iconic, animal-dwelling bacterial family, we examined 42 publicly available genomes cultured uncultured strains for presence chitinase-encoding genes....

10.1038/s43705-023-00316-7 article EN cc-by ISME Communications 2023-10-14

This work describes the extraction and back-extraction of a lipase from crude extract Penicillium citrinum using AOT reversed micelles in isooctane. The effect pH, ionic strength, concentration on protein forward backward transfer at 20°C was studied. maximum (32·0%) achieved pH 4·0 with 50 mmol dm−3 acetate buffer containing 100 KCl Proteins were back-extracted (82·7%) to new aqueous phase 8·0 phosphate 1000 KCl. No enzyme activity could be detected either micellar or after back-extraction....

10.1002/(sici)1097-4660(199705)69:1<77::aid-jctb666>3.0.co;2-v article EN Journal of Chemical Technology & Biotechnology 1997-05-01

The cutinase from Fusarium solani pisi is an enzyme with a single l-tryptophan (Trp) involved in hydrogen bond alanine (Ala) residue and located close to cystine formed by disulfide bridge between two cysteine (Cys) residues. Cys strongly quenches the fluorescence of Trp both static dynamic quenching mechanisms. intensity increases about fourfold on protein melting because disruption Ala–Trp that releases vicinity residue. forms charge–transfer complexes bridge, which disrupted UV light...

10.1562/0031-8655(2003)0780015fotsto2.0.co2 article EN Photochemistry and Photobiology 2007-05-01

Abstract A new methodology for the rapid assessment of affinity ligands synthesized by combinatorial solid‐phase chemistry is reported. This screening strategy utilizes target protein conjugated to FITC, and represents an almost universal technique preliminary libraries. The a triazine‐scaffolded library ligands, designed bind human IgG, was performed with FITC‐human results compared those obtained conventional chromatographic assays. effect different molar conjugation ratios FITC–IgG (F/P)...

10.1002/jmr.661 article EN Journal of Molecular Recognition 2004-04-27

The cutinase from Fusarium solani pisi is an enzyme with a single l-tryptophan (Trp) involved in hydrogen bond alanine (Ala) residue and located close to cystine formed by disulfide bridge between two cysteine (Cys) residues. Cys strongly quenches the fluorescence of Trp both static dynamic quenching mechanisms. intensity increases about fourfold on protein melting because disruption Ala–Trp that releases vicinity residue. forms charge–transfer complexes bridge, which disrupted UV light...

10.1562/0031-8655(2003)078<0015:fotsto>2.0.co;2 article EN Photochemistry and Photobiology 2003-01-01

Cutinase from Fusarium solani pisi is an enzyme that bridges functional properties between lipases and esterases, with applications in detergents, food processing, the synthesis of fine chemicals. The purification procedure recombinant cutinase E. coil extracts a well-established but time-consuming process, which involves sequence two anionic exchange chromatography steps followed by dialysis. Affinity most efficient method for protein purification, major limitation its use being often...

10.3390/biomimetics9010057 article EN cc-by Biomimetics 2024-01-20

Biomimetic ligands are synthetic compounds that mimic the structure and binding properties of natural biological ligands. The first uses textile dyes as pseudo-affinity paved way for rational design de novo synthesis low-cost, non-toxic highly stable triazine-scaffolded affinity A novel method to assess enhance protein stability, employing triazine-based biomimetic using cutinase from Fusarium solani pisi a model, has been previously reported. This innovative approach combined concepts...

10.3390/pr12020371 article EN Processes 2024-02-11
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