Colloidal lignin particles as adhesives for soft materials

Maija Liisa Mattinen (Corresponding Author), Guillaume Riviere, Alexander Henn, Robertus Wahyu N. Nugroho, Timo Leskinen, Outi Nivala, Juan José Valle-Delgado, Mauri A. Kostiainen, Monika Österberg

    Research output: Contribution to journalArticleScientificpeer-review

    31 Citations (Scopus)


    Lignin has interesting functionalities to be exploited in adhesives for medicine, foods and textiles. Nanoparticles (NPs) < 100 nm coated with poly (L-lysine), PL and poly(L-glutamic acid) PGA were prepared from the laccase treated lignin to coat nanocellulose fibrils (CNF) with heat. NPs ca. 300 nm were prepared, β-casein coated and cross-linked with transglutaminase (Tgase) to agglutinate chamois. Size exclusion chromatography (SEC) and Fourier-transform infrared (FTIR) spectroscopy were used to characterize polymerized lignin, while zeta potential and dynamic light scattering (DLS) to ensure coating of colloidal lignin particles (CLPs). Protein adsorption on lignin was studied by quartz crystal microbalance (QCM). Atomic force microscopy (AFM) was exploited to examine interactions between different polymers and to image NPs with transmission electron microscopy (TEM). Tensile testing showed, when using CLPs for the adhesion, the stress improved ca. 10 and strain ca. 6 times compared to unmodified Kraft. For the β-casein NPs, the values were 20 and 8, respectively, and for the β-casein coated CLPs between these two cases. When NPs were dispersed in adhesive formulation, the increased Young’s moduli confirmed significant improvement in the stiffness of the joints over the adhesive alone. Exploitation of lignin in nanoparticulate morphology is a potential method to prepare bionanomaterials for advanced applications.

    Original languageEnglish
    Article number1001
    Issue number12
    Publication statusPublished - 2018
    MoE publication typeNot Eligible


    • Cross-link
    • Enzyme
    • Fibril
    • Heat
    • Lignin
    • Nanocellulose
    • Nanoparticle
    • Protein
    • Self-assembly


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