Adhesion and tribological properties of hydrophobin proteins in aqueous lubrication on stainless steel surfaces

Timo J. Hakala (Corresponding Author), Päivi Laaksonen, Vesa Saikko, Tiina Ahlroos, Aino Helle, Riitta Mahlberg, Hendrik Hähl, Karin Jacobs, Petri Kuosmanen, Markus, B. Linder, Kenneth Holmberg

    Research output: Contribution to journalArticleScientificpeer-review

    25 Citations (Scopus)

    Abstract

    Macroscale tribological properties of hydrophobin layers bound on stainless steel surfaces were investigated in an aqueous environment. Emphasis was on boundary lubrication because water easily fails in hydrodynamic lubrication due to its low viscosity. We studied the affinities of two different proteins, HFBI and FpHYD5, on stainless steel and their ability to bind water at the surface by combining quartz crystal microbalance (QCM-D) and ellipsometry. Both proteins contained an adhesive hydrophobic domain, but FpHYD5 also had a very strongly hydrating carbohydrate structure attached to it. The lubrication properties of the proteins were studied with two different methods, pin-on-disc (POD) (stainless steel vs. stainless steel) and circular translation pin-on-disc (CTPOD) (UHMWPE vs. stainless steel). It was observed that both hydrophobins could adhere to the stainless steel surface and form highly hydrated layers. Both proteins reduced friction and wear of the sliding contact between two stainless steel surfaces. With UHMWPE against stainless steel, the hydrophobins prevented the polyethylene transfer to the counterface. The lowest coefficient of friction (COF) 0.13 was observed when FpHYD5 hydrophobins were employed in pure water. On the other hand, the lowest wear was observed when FpHYD5 proteins were added in a 50 mM sodium acetate buffer. Increasing the water content and loosening the hydrophobin film structure on the stainless steel surface led to a reduction in friction and wear.
    Original languageEnglish
    Pages (from-to)9867-9872
    Number of pages5
    JournalRSC Advances
    Volume2
    Issue number26
    DOIs
    Publication statusPublished - 2012
    MoE publication typeA1 Journal article-refereed

    Fingerprint

    Stainless Steel
    Lubrication
    Adhesion
    Stainless steel
    Proteins
    Ultrahigh molecular weight polyethylenes
    Wear of materials
    Friction
    Water
    Sodium Acetate
    Quartz crystal microbalances
    Ellipsometry
    Polyethylene
    Carbohydrates
    Water content
    Polyethylenes
    Adhesives
    Buffers
    Hydrodynamics
    Sodium

    Keywords

    • Water lubrication
    • hydrophobins
    • friction

    Cite this

    Hakala, Timo J. ; Laaksonen, Päivi ; Saikko, Vesa ; Ahlroos, Tiina ; Helle, Aino ; Mahlberg, Riitta ; Hähl, Hendrik ; Jacobs, Karin ; Kuosmanen, Petri ; Linder, Markus, B. ; Holmberg, Kenneth. / Adhesion and tribological properties of hydrophobin proteins in aqueous lubrication on stainless steel surfaces. In: RSC Advances. 2012 ; Vol. 2, No. 26. pp. 9867-9872.
    @article{2ee050b5def24b9080de70820853faeb,
    title = "Adhesion and tribological properties of hydrophobin proteins in aqueous lubrication on stainless steel surfaces",
    abstract = "Macroscale tribological properties of hydrophobin layers bound on stainless steel surfaces were investigated in an aqueous environment. Emphasis was on boundary lubrication because water easily fails in hydrodynamic lubrication due to its low viscosity. We studied the affinities of two different proteins, HFBI and FpHYD5, on stainless steel and their ability to bind water at the surface by combining quartz crystal microbalance (QCM-D) and ellipsometry. Both proteins contained an adhesive hydrophobic domain, but FpHYD5 also had a very strongly hydrating carbohydrate structure attached to it. The lubrication properties of the proteins were studied with two different methods, pin-on-disc (POD) (stainless steel vs. stainless steel) and circular translation pin-on-disc (CTPOD) (UHMWPE vs. stainless steel). It was observed that both hydrophobins could adhere to the stainless steel surface and form highly hydrated layers. Both proteins reduced friction and wear of the sliding contact between two stainless steel surfaces. With UHMWPE against stainless steel, the hydrophobins prevented the polyethylene transfer to the counterface. The lowest coefficient of friction (COF) 0.13 was observed when FpHYD5 hydrophobins were employed in pure water. On the other hand, the lowest wear was observed when FpHYD5 proteins were added in a 50 mM sodium acetate buffer. Increasing the water content and loosening the hydrophobin film structure on the stainless steel surface led to a reduction in friction and wear.",
    keywords = "Water lubrication, hydrophobins, friction",
    author = "Hakala, {Timo J.} and P{\"a}ivi Laaksonen and Vesa Saikko and Tiina Ahlroos and Aino Helle and Riitta Mahlberg and Hendrik H{\"a}hl and Karin Jacobs and Petri Kuosmanen and Linder, {Markus, B.} and Kenneth Holmberg",
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    doi = "10.1039/C2RA21018E",
    language = "English",
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    pages = "9867--9872",
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    Hakala, TJ, Laaksonen, P, Saikko, V, Ahlroos, T, Helle, A, Mahlberg, R, Hähl, H, Jacobs, K, Kuosmanen, P, Linder, MB & Holmberg, K 2012, 'Adhesion and tribological properties of hydrophobin proteins in aqueous lubrication on stainless steel surfaces', RSC Advances, vol. 2, no. 26, pp. 9867-9872. https://doi.org/10.1039/C2RA21018E

    Adhesion and tribological properties of hydrophobin proteins in aqueous lubrication on stainless steel surfaces. / Hakala, Timo J. (Corresponding Author); Laaksonen, Päivi; Saikko, Vesa; Ahlroos, Tiina; Helle, Aino; Mahlberg, Riitta; Hähl, Hendrik; Jacobs, Karin; Kuosmanen, Petri; Linder, Markus, B.; Holmberg, Kenneth.

    In: RSC Advances, Vol. 2, No. 26, 2012, p. 9867-9872.

    Research output: Contribution to journalArticleScientificpeer-review

    TY - JOUR

    T1 - Adhesion and tribological properties of hydrophobin proteins in aqueous lubrication on stainless steel surfaces

    AU - Hakala, Timo J.

    AU - Laaksonen, Päivi

    AU - Saikko, Vesa

    AU - Ahlroos, Tiina

    AU - Helle, Aino

    AU - Mahlberg, Riitta

    AU - Hähl, Hendrik

    AU - Jacobs, Karin

    AU - Kuosmanen, Petri

    AU - Linder, Markus, B.

    AU - Holmberg, Kenneth

    N1 - Project code: 34126 Project code: 41202

    PY - 2012

    Y1 - 2012

    N2 - Macroscale tribological properties of hydrophobin layers bound on stainless steel surfaces were investigated in an aqueous environment. Emphasis was on boundary lubrication because water easily fails in hydrodynamic lubrication due to its low viscosity. We studied the affinities of two different proteins, HFBI and FpHYD5, on stainless steel and their ability to bind water at the surface by combining quartz crystal microbalance (QCM-D) and ellipsometry. Both proteins contained an adhesive hydrophobic domain, but FpHYD5 also had a very strongly hydrating carbohydrate structure attached to it. The lubrication properties of the proteins were studied with two different methods, pin-on-disc (POD) (stainless steel vs. stainless steel) and circular translation pin-on-disc (CTPOD) (UHMWPE vs. stainless steel). It was observed that both hydrophobins could adhere to the stainless steel surface and form highly hydrated layers. Both proteins reduced friction and wear of the sliding contact between two stainless steel surfaces. With UHMWPE against stainless steel, the hydrophobins prevented the polyethylene transfer to the counterface. The lowest coefficient of friction (COF) 0.13 was observed when FpHYD5 hydrophobins were employed in pure water. On the other hand, the lowest wear was observed when FpHYD5 proteins were added in a 50 mM sodium acetate buffer. Increasing the water content and loosening the hydrophobin film structure on the stainless steel surface led to a reduction in friction and wear.

    AB - Macroscale tribological properties of hydrophobin layers bound on stainless steel surfaces were investigated in an aqueous environment. Emphasis was on boundary lubrication because water easily fails in hydrodynamic lubrication due to its low viscosity. We studied the affinities of two different proteins, HFBI and FpHYD5, on stainless steel and their ability to bind water at the surface by combining quartz crystal microbalance (QCM-D) and ellipsometry. Both proteins contained an adhesive hydrophobic domain, but FpHYD5 also had a very strongly hydrating carbohydrate structure attached to it. The lubrication properties of the proteins were studied with two different methods, pin-on-disc (POD) (stainless steel vs. stainless steel) and circular translation pin-on-disc (CTPOD) (UHMWPE vs. stainless steel). It was observed that both hydrophobins could adhere to the stainless steel surface and form highly hydrated layers. Both proteins reduced friction and wear of the sliding contact between two stainless steel surfaces. With UHMWPE against stainless steel, the hydrophobins prevented the polyethylene transfer to the counterface. The lowest coefficient of friction (COF) 0.13 was observed when FpHYD5 hydrophobins were employed in pure water. On the other hand, the lowest wear was observed when FpHYD5 proteins were added in a 50 mM sodium acetate buffer. Increasing the water content and loosening the hydrophobin film structure on the stainless steel surface led to a reduction in friction and wear.

    KW - Water lubrication

    KW - hydrophobins

    KW - friction

    U2 - 10.1039/C2RA21018E

    DO - 10.1039/C2RA21018E

    M3 - Article

    VL - 2

    SP - 9867

    EP - 9872

    JO - RSC Advances

    JF - RSC Advances

    SN - 2046-2069

    IS - 26

    ER -