Leila Lo Leggio

Leila Lo Leggio

Professor


  1. 2023
  2. Published

    AA16 Oxidoreductases Boost Cellulose-Active AA9 Lytic Polysaccharide Monooxygenases from Myceliophthora thermophila

    Sun, P., Huang, Zhiyu, Banerjee, S., Kadowaki, M. A. S., Veersma, R. J., Magri, S., Hilgers, R., Muderspach, Sebastian Jannick, Laurent, C. V. F. P., Ludwig, R., Cannella, D., Lo Leggio, Leila, van Berkel, W. J. H. & Kabel, M. A., 2023, In: ACS Catalysis. 13, 7, p. 4454-4467 14 p.

    Research output: Contribution to journalJournal articleResearchpeer-review

  3. Published

    Glucuronoyl esterases – enzymes to decouple lignin and carbohydrates and enable better utilization of renewable plant biomass

    Larsbrink, J. & Lo Leggio, Leila, 2023, In: Essays in Biochemistry. 67, 3, p. 493-503 11 p.

    Research output: Contribution to journalReviewResearchpeer-review

  4. Published

    Joint X-ray/neutron structure of Lentinus similis AA9_A at room temperature

    Tandrup, T., Lo Leggio, Leila & Meilleur, F., 2023, In: Acta crystallographica. Section F, Structural biology communications. 79, 1, p. 1-7 7 p.

    Research output: Contribution to journalJournal articleResearchpeer-review

  5. Published

    Structural and functional investigation of a fungal member of carbohydrate esterase family 15 with potential specificity for rare xylans

    Mazurkewich, S., Scholzen, K. C., Brusch, R. H., Poulsen, Jens-Christian Navarro, Theibich, Yusuf, Hüttner, S., Olsson, L., Larsbrink, J. & Lo Leggio, Leila, 2023, In: Acta crystallographica. Section D, Structural biology. 79, 6, p. 545-555 11 p.

    Research output: Contribution to journalJournal articleResearchpeer-review

  6. Published

    Structure, function, and protein engineering of GH53 β-1,4-galactanases

    Muderspach, Sebastian Jannick, Jensen, K., Krogh, K. B. R. M. & Lo Leggio, Leila, 2023, Glycoside Hydrolases: Biochemistry, Biophysics, and Biotechnology. Elsevier, p. 295-322 28 p.

    Research output: Chapter in Book/Report/Conference proceedingBook chapterResearchpeer-review

ID: 13810