Enzymatic cross-linking of gelatine with laccase and tyrosinase

被引：34

作者：

Jus, Suzana ^{[1
]}

Stachel, Ines ^{[2
]}

Fairhead, Michael ^{[3
]}

Meyer, Michael ^{[2
]}

Thoeny-Meyer, Linda ^{[3
]}

Guebitz, Georg M. ^{[1
]}

机构：

[1] Graz Univ Technol, Inst Environm Biotechnol, A-8010 Graz, Austria

[2] Forschungsinst Leder & Kunststoffbahnen gGmbH, Freiberg, Germany

[3] Empa, Swiss Fed Labs Mat Testing & Res, Lab Biomat, St Gallen, Switzerland

来源：

BIOCATALYSIS AND BIOTRANSFORMATION | 2012年 / 30卷 / 01期

关键词：

gelatine; laccase; tyrosinase; CATALYZED CONJUGATION; LINKED GELATIN; PROTEIN; COLLAGEN; POLYMERIZATION; PEROXIDASE; FOOD; OXIDATION; HYDROGELS; PROPERTY;

D O I：

10.3109/10242422.2012.646036

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：86 / 95

页数：10

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