Improving laccase catalyzed cross-linking of whey protein isolate and their application as emulsifiers

Hairan Ma, Pirkko Forssell, Riitta Partanen, Johanna Buchert, Harry Boer (Corresponding Author)

Research output: Contribution to journalArticleScientificpeer-review

36 Citations (Scopus)

Abstract

Whey protein isolate (WPI) was chemically modified by vanillic acid in order to enhance its cross-linkability by laccase enzyme. Incorporation of methoxyphenol groups created reactive sites for laccase on the surface of the protein and improved the efficiency of cross-linking. The vanillic acid modified WPI (Van-WPI) was characterized using MALDI-TOF mass spectrometry, and the laccase-catalyzed cross-linking of Van-WPI was studied. Furthermore, the vanillic acid modification was compared with the conventional approach to improve laccase-catalyzed cross-linking by adding free phenolic compounds. A small extent of the vanillic acid modification significantly improved the cross-linkability of the protein and made it possible to avoid color formation in a system that is free of small phenolic compounds. Moreover, the potential application of Van-WPI as emulsifier and the effect of cross-linking on the stability of Van-WPI emulsion were investigated. The post-emulsification cross-linking by laccase was proven to enhance the storage stability of Van-WPI emulsion.
Original languageEnglish
Pages (from-to)1406-1414
Number of pages9
JournalJournal of Agricultural and Food Chemistry
Volume59
Issue number4
DOIs
Publication statusPublished - 2011
MoE publication typeA1 Journal article-refereed

Fingerprint

Vanillic Acid
Laccase
vanillic acid
whey protein isolate
laccase
emulsifiers
crosslinking
Proteins
Emulsions
emulsions
phenolic compounds
Emulsification
Whey Proteins
matrix-assisted laser desorption-ionization mass spectrometry
Matrix-Assisted Laser Desorption-Ionization Mass Spectrometry
surface proteins
emulsifying
active sites
Mass spectrometry
Mass Spectrometry

Keywords

  • Vanillic acid modification
  • cross-linkability
  • color formation
  • emulsion
  • stability
  • post-emulsification cross-linking

Cite this

Ma, Hairan ; Forssell, Pirkko ; Partanen, Riitta ; Buchert, Johanna ; Boer, Harry. / Improving laccase catalyzed cross-linking of whey protein isolate and their application as emulsifiers. In: Journal of Agricultural and Food Chemistry. 2011 ; Vol. 59, No. 4. pp. 1406-1414.
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Improving laccase catalyzed cross-linking of whey protein isolate and their application as emulsifiers. / Ma, Hairan; Forssell, Pirkko; Partanen, Riitta; Buchert, Johanna; Boer, Harry (Corresponding Author).

In: Journal of Agricultural and Food Chemistry, Vol. 59, No. 4, 2011, p. 1406-1414.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Improving laccase catalyzed cross-linking of whey protein isolate and their application as emulsifiers

AU - Ma, Hairan

AU - Forssell, Pirkko

AU - Partanen, Riitta

AU - Buchert, Johanna

AU - Boer, Harry

PY - 2011

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N2 - Whey protein isolate (WPI) was chemically modified by vanillic acid in order to enhance its cross-linkability by laccase enzyme. Incorporation of methoxyphenol groups created reactive sites for laccase on the surface of the protein and improved the efficiency of cross-linking. The vanillic acid modified WPI (Van-WPI) was characterized using MALDI-TOF mass spectrometry, and the laccase-catalyzed cross-linking of Van-WPI was studied. Furthermore, the vanillic acid modification was compared with the conventional approach to improve laccase-catalyzed cross-linking by adding free phenolic compounds. A small extent of the vanillic acid modification significantly improved the cross-linkability of the protein and made it possible to avoid color formation in a system that is free of small phenolic compounds. Moreover, the potential application of Van-WPI as emulsifier and the effect of cross-linking on the stability of Van-WPI emulsion were investigated. The post-emulsification cross-linking by laccase was proven to enhance the storage stability of Van-WPI emulsion.

AB - Whey protein isolate (WPI) was chemically modified by vanillic acid in order to enhance its cross-linkability by laccase enzyme. Incorporation of methoxyphenol groups created reactive sites for laccase on the surface of the protein and improved the efficiency of cross-linking. The vanillic acid modified WPI (Van-WPI) was characterized using MALDI-TOF mass spectrometry, and the laccase-catalyzed cross-linking of Van-WPI was studied. Furthermore, the vanillic acid modification was compared with the conventional approach to improve laccase-catalyzed cross-linking by adding free phenolic compounds. A small extent of the vanillic acid modification significantly improved the cross-linkability of the protein and made it possible to avoid color formation in a system that is free of small phenolic compounds. Moreover, the potential application of Van-WPI as emulsifier and the effect of cross-linking on the stability of Van-WPI emulsion were investigated. The post-emulsification cross-linking by laccase was proven to enhance the storage stability of Van-WPI emulsion.

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