期刊
BIOCATALYSIS AND BIOTRANSFORMATION
卷 30, 期 1, 页码 86-95出版社
TAYLOR & FRANCIS LTD
DOI: 10.3109/10242422.2012.646036
关键词
gelatine; laccase; tyrosinase
资金
- German Ministry of Economy
- OeGMBT
- Austrian Federal Ministry of Economy, Family and Youth (BMWFJ)
- Federal Ministry of Traffic, Innovation and Technology (bmvit)
- Styrian Business Promotion Agency SFG
- Standortagentur Tirol and ZIT - Technology Agency of the City of Vienna
- MacroFun project
- COST Action [868]
- EU
Conventional cross-linking of proteins involves the use of toxic chemicals. Here, cross-linking of gelatine and gelatine hydrolysates with tyrosinases from Botryosphaeria obtusa (BoT1 and BoT2), Agaricus bisporus (AbT) and from Verrucomicrobium spinosum (VsT) and with laccases from Trametes hirsuta (ThL) and T. versicolor (TvL) was demonstrated. Enzymatic oxidation of tyrosine residues was indicated by UV/VIS and fluorescence spectroscopy and further confirmed by oxygen consumption measurements. Using a model substrate (Tyr-Ala) dimerization was demonstrated by using RP-HPLC and LC-MS. Enzymatic cross-linking significantly increased the molecular weight of the soluble material up to the point of precipitation as demonstrated by both SDS-PAGE and size exclusion chromatography. The effect of cross-linking was further enhanced in the presence of phenolic molecules such as catechin.
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