Directing enzymatic cross-linking activity to the air-water interface by a fusion protein approach

Arja Paananen (Corresponding Author), Dilek Ercili Cura, Markku Saloheimo, Raija Lantto, Markus Linder

Research output: Contribution to journalArticleScientificpeer-review

9 Citations (Scopus)

Abstract

Enzymatic cross-linking of proteins is of great interest due to an effective and controlled way of modifying the structures of protein networks. Enzyme-aided structural engineering aims at enhanced stabilisation of foams, emulsions and dispersions by enzymatically inducing intra- and intermolecular cross-links between proteins in continuous phase and/or at interfaces. Formation of stronger interfacial structures protects air bubbles or oil droplets against coalescence, and in some applications, may even be preferable to bulk reactions. In this work we studied direction of enzymatic cross-linking reactions to the air–water interface by enhancing the functionality of enzymes as fusion proteins. We used a hydrophobin–laccase fusion protein, HFBI–MaL, where the surface active hydrophobin component facilitates the access for laccase to cross-link β-casein film directly at the air–water interface. As a result, enhanced cross-linking was shown by means of surface dilatational rheology, where increased G moduli indicated formation of a stronger film with the fusion protein compared to native laccase.
Original languageEnglish
Pages (from-to)1612-1619
Number of pages8
JournalSoft Matter
Volume9
Issue number5
DOIs
Publication statusPublished - 2013
MoE publication typeA1 Journal article-refereed

Fingerprint

Fusion reactions
fusion
proteins
Water
air
Laccase
Air
water
Proteins
enzymes
structural engineering
Enzymes
Caseins
Emulsions
Bubbles (in fluids)
Coalescence
Dispersions
Rheology
Structural design
Foams

Cite this

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title = "Directing enzymatic cross-linking activity to the air-water interface by a fusion protein approach",
abstract = "Enzymatic cross-linking of proteins is of great interest due to an effective and controlled way of modifying the structures of protein networks. Enzyme-aided structural engineering aims at enhanced stabilisation of foams, emulsions and dispersions by enzymatically inducing intra- and intermolecular cross-links between proteins in continuous phase and/or at interfaces. Formation of stronger interfacial structures protects air bubbles or oil droplets against coalescence, and in some applications, may even be preferable to bulk reactions. In this work we studied direction of enzymatic cross-linking reactions to the air–water interface by enhancing the functionality of enzymes as fusion proteins. We used a hydrophobin–laccase fusion protein, HFBI–MaL, where the surface active hydrophobin component facilitates the access for laccase to cross-link β-casein film directly at the air–water interface. As a result, enhanced cross-linking was shown by means of surface dilatational rheology, where increased G moduli indicated formation of a stronger film with the fusion protein compared to native laccase.",
author = "Arja Paananen and {Ercili Cura}, Dilek and Markku Saloheimo and Raija Lantto and Markus Linder",
year = "2013",
doi = "10.1039/c2sm27234b",
language = "English",
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pages = "1612--1619",
journal = "Soft Matter",
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publisher = "Royal Society of Chemistry RSC",
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Directing enzymatic cross-linking activity to the air-water interface by a fusion protein approach. / Paananen, Arja (Corresponding Author); Ercili Cura, Dilek; Saloheimo, Markku; Lantto, Raija; Linder, Markus.

In: Soft Matter, Vol. 9, No. 5, 2013, p. 1612-1619.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Directing enzymatic cross-linking activity to the air-water interface by a fusion protein approach

AU - Paananen, Arja

AU - Ercili Cura, Dilek

AU - Saloheimo, Markku

AU - Lantto, Raija

AU - Linder, Markus

PY - 2013

Y1 - 2013

N2 - Enzymatic cross-linking of proteins is of great interest due to an effective and controlled way of modifying the structures of protein networks. Enzyme-aided structural engineering aims at enhanced stabilisation of foams, emulsions and dispersions by enzymatically inducing intra- and intermolecular cross-links between proteins in continuous phase and/or at interfaces. Formation of stronger interfacial structures protects air bubbles or oil droplets against coalescence, and in some applications, may even be preferable to bulk reactions. In this work we studied direction of enzymatic cross-linking reactions to the air–water interface by enhancing the functionality of enzymes as fusion proteins. We used a hydrophobin–laccase fusion protein, HFBI–MaL, where the surface active hydrophobin component facilitates the access for laccase to cross-link β-casein film directly at the air–water interface. As a result, enhanced cross-linking was shown by means of surface dilatational rheology, where increased G moduli indicated formation of a stronger film with the fusion protein compared to native laccase.

AB - Enzymatic cross-linking of proteins is of great interest due to an effective and controlled way of modifying the structures of protein networks. Enzyme-aided structural engineering aims at enhanced stabilisation of foams, emulsions and dispersions by enzymatically inducing intra- and intermolecular cross-links between proteins in continuous phase and/or at interfaces. Formation of stronger interfacial structures protects air bubbles or oil droplets against coalescence, and in some applications, may even be preferable to bulk reactions. In this work we studied direction of enzymatic cross-linking reactions to the air–water interface by enhancing the functionality of enzymes as fusion proteins. We used a hydrophobin–laccase fusion protein, HFBI–MaL, where the surface active hydrophobin component facilitates the access for laccase to cross-link β-casein film directly at the air–water interface. As a result, enhanced cross-linking was shown by means of surface dilatational rheology, where increased G moduli indicated formation of a stronger film with the fusion protein compared to native laccase.

U2 - 10.1039/c2sm27234b

DO - 10.1039/c2sm27234b

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VL - 9

SP - 1612

EP - 1619

JO - Soft Matter

JF - Soft Matter

SN - 1744-683X

IS - 5

ER -