Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.10.3.1 (tyrosinase)
 9,065 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Oat and faba bean protein isolates were treated with transglutaminase from Streptomyces mobaraensis and tyrosinase from Trichoderma reesei to modify the colloidal properties of protein particles in order to improve their colloidal stability and foaming properties. Transglutaminase crosslinked faba bean protein extensively already with 10nkat/g enzyme dosage. Oat protein was crosslinked to some extent with transglutaminase with higher dosages (100 and 1000nkat/g). Transglutaminase increased the absolute zeta-potential values and reduced the particle size of oat protein particles. As a result, the colloidal stability and foaming properties were improved. Tyrosinase had limited crosslinking ability on both plant protein materials. Tyrosinase greatly reduced the solubility of oat protein despite limited crosslinking. Tyrosinase did not have effect on zeta-potential or colloidal stability of either protein, but it impaired foaming properties of both. Thus, the crosslinking enzymes studied caused significantly different end product functionality, presumably due to the different mechanism of action.
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PMID:Structuring colloidal oat and faba bean protein particles via enzymatic modification. 2845 27

Tropomyosin (TM) is the major allergen in shellfish, which causes severe food allergy worldwide and shows wide cross-reactivity in different species. Transglutaminase (TG) and tyrosinase (Tyr) are protein modification enzymes that catalyze substrate cross-linking and change protein structures and properties. The aim of this work was to investigate the effect of TG and Tyr on TM. After TG/Tyr treatment, the cross-linking and protein structural change were observed by SDS-PAGE, scanning electron microscopy and circular dichroism. Furthermore, ELISA and mast cell degranulation assay with allergic sera demonstrated the allergenicity reduction after treatment. An in vivo TM-sensitization mouse model showed that both TG and Tyr treatments reduced the IgE-induction capacity of TM but maintained the IgG-induction ability, making the treated TM a potential hypoallergen. Moreover, TG-but-not-Tyr-treated TM promoted regulatory T cell proliferation and thus may facilitate the establishment of oral tolerance. This work provided an effective method to reduce TM allergenicity and produce hypoallergens, which has broad application prospects in low allergenic food production and allergen-specific immunotherapy.
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PMID:Cross-linking of shrimp tropomyosin catalyzed by transglutaminase and tyrosinase produces hypoallergens for potential immunotherapy. 3082 May 2