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

43 Citations (Scopus)


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
Issue number4
Publication statusPublished - 2011
MoE publication typeA1 Journal article-refereed


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

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