Enzymatic cross-linking of proteins with tyrosinase

Thalmann, Claudia Rita; Lötzbeyer, Thomas

doi:10.1007/s00217-001-0455-0

Cited by 112 publications

(93 citation statements)

References 3 publications

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“…Emmambux et al (2004) applied extensive heating (at 55 to 75°C range) to zein-tannic acid mixtures during both film preparation and drying. Thus, it is also possible that the antiplasticizing effect was due to oxidation of TA which could cause covalent crosslinking of proteins (Thalmann & Lötzbeyer, 2002). Another study which employed a pure phenolic compound during edible film production came from Ku, Hong, and Song (2008), but these workers incorporated the phenolic compound catechin into a carbohydrate film from agar extracted from Gelidium corneum and did not determine any plasticizing effect of catechin.…”

Section: Effect Of Phenolic Compounds On Mechanical Properties Of Filmsmentioning

confidence: 99%

Incorporating phenolic compounds opens a new perspective to use zein films as flexible bioactive packaging materials

Arcan

Yemenicioğlu

2011

Food Research International

194

108

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To eliminate their classical brittleness and flexibility problems zein films were plasticized by incorporation of different phenolic acids (gallic acid (GA), p-hydroxy benzoic acid (HBA) or ferulic acids (FA)) or flavonoids (catechin (CAT), flavone (FLA) or quercetin (QU)). The use of GA, CAT, FA and HBA at 3 mg/cm 2 eliminated the brittleness of films and gave highly flexible films showing elongations between 135% and 189%, while FLA and QU caused no considerable effect on film elongation. The films containing FA and HBA showed extreme swelling and lost their structural integrity when hydrated in distilled water. In contrast, CAT and GA containing films maintained their integrity following hydration. Most of the GA (up to 93%) and a considerable portion of CAT (up to 60%) in the films existed in soluble form. Therefore, the films showed antioxidant and/or antimicrobial activity. The TEACs of soluble phenolic compounds in 3 mg/cm 2 CAT and GA containing films were 21.0 and 86.2 μmol trolox/cm 2 , respectively. The GA containing films showed antimicrobial activity on Listeria monocytogenes and Campylobacter jejuni, while CAT showed no antimicrobial activity on these bacteria at the studied concentration. This work opens a new perspective for using zein in flexible bioactive packaging.

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Section: Effect Of Phenolic Compounds On Mechanical Properties Of Filmsmentioning

confidence: 99%

Incorporating phenolic compounds opens a new perspective to use zein films as flexible bioactive packaging materials

Arcan

Yemenicioğlu

2011

Food Research International

194

108

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“…It is the enzyme responsible for the production of melanin in organisms and its native substrate is L-tyrosine. Tyrosinases from different origins have been investigated for their protein crosslinking ability on milk and wheat proteins, but not on soy glycinin (Heijnis, Wierenga, van Berkel, & Gruppen, 2010;Selinheimo, Autio, Kruus, & Buchert, 2007;Thalmann & L€ otzbeyer, 2002). Studies demonstrated that the crosslinking ability of tyrosinase is limited by the structure of the substrate protein and the exposure of its tyrosine residues and in most cases, required a low molecular weight phenolic agent as a mediator ( Fig.…”

Section: Introductionmentioning

confidence: 99%

“…Studies demonstrated that the crosslinking ability of tyrosinase is limited by the structure of the substrate protein and the exposure of its tyrosine residues and in most cases, required a low molecular weight phenolic agent as a mediator ( Fig. 1) (Heck, Faccio, Richter, & Th€ ony-Meyer, 2013;Thalmann & L€ otzbeyer, 2002).…”

Section: Introductionmentioning

confidence: 99%

Characterization of oil-in-water emulsions stabilized by tyrosinase-crosslinked soy glycinin

et al. 2015

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a b s t r a c tThe effect of crosslinked soy glycinin with tyrosinase from Bacillus megaterium (TyrBm) on o/w emulsion properties was studied. The ability of TyrBm to crosslink soy glycinin was evaluated in the presence or absence of three phenolic mediators. It was observed that crosslinking of glycinin is facilitated by a phenolic mediator and is negligible in its absence. Subsequently, the glycinin-stabilized emulsions were evaluated in two systems: (i) homogenization after crosslinking in the presence of a mediator, caffeic acid, and (ii) homogenization prior to crosslinking in the absence of caffeic acid. Emulsions were prepared using a high-pressure homogenizer and their particle size, creaming resistance, viscosity and microstructure were measured. Results indicate that the method of emulsion preparation affected the emulsion physical stability, thus, the first system led to a decrease in emulsion stability against creaming while the second system resulted with improved properties after the enzymatic treatment; Crosslinking after homogenization eliminated the need for a phenolic mediator and led to a lower creaming velocity and higher viscosity. In addition, fluorescence microscopy observations demonstrated that the crosslinking reaction of TyrBm after homogenization led to the formation of cold-set gel-like structures of small droplets linked by covalent bonds.

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“…Mushrooms are widely used as a potent PPO source as they are readily obtained in relatively large quantities and are inexpensive [3]. In food industry, the use of mushroom PPO was found to be valuable for removal of the astringent and bitter taste of cocoa beans [14] and enzymatic cross-linking of proteins as an alternative to the already established use of transglutaminase [15]. The enzyme shows sufficient monophenolase activity essential for its technological applications in such cases as biosynthesis of o-diphenolic antioxidant hydroxytyrosol in an environmentally friendly manner [16] and food colorants such as red-violet betalains and gold colored aurons [17].…”

Section: Introductionmentioning

confidence: 99%

Partial purification and kinetic characterization of mushroom stem polyphenoloxidase and determination of its storage stability in different lyophilized forms

Şimşek¹,

Yemenicioğlu²

2007

Process Biochemistry

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Monophenolase (1011 AE 626 U/g AP) and diphenolase activities (5163 AE 3059 U/g AP) of PPO in acetone powders (APs) of different mushroom stems varied considerably. However, the limited variation of average dipenolase (L-DOPA) to monophenolase (L-tyrosine) activity ratio (5.4 AE 0.7) in crude extracts showed the homogeneity of PPO from different mushroom stems. The change in extraction material or partial purification method (ammonium sulfate or acetone precipitation) did not affect the temperature stability, temperature and pH dependency and K m of monophenolase activity considerably. However, some changes were observed in pH stability and substrate specificity of PPO in different parties of mushroom stems. The most important aspects of mushroom stem PPO are its lower diphenolase to monophenolase activity ratio than mushroom cap PPO, low temperature dependency of activity between 25 and 40 8C (E a = 30 kJ/mol), broad optimum pH between 6 and 8, but lack of activity pH 5, and ability to use phloridzin as substrate. The mushroom stem PPOs partially purified and lyophilized by using sucrose, dextran or alginate showed moderate to high stability at À18 8C for 6-6.5 months. Thus, the mushroom stems obtained as a waste material during mushroom processing may be used as a more homogenous source than whole mushrooms to obtain PPO used for different industrial, clinical or research purposes. #

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Enzymatic cross-linking of proteins with tyrosinase

Cited by 112 publications

References 3 publications

Incorporating phenolic compounds opens a new perspective to use zein films as flexible bioactive packaging materials

Incorporating phenolic compounds opens a new perspective to use zein films as flexible bioactive packaging materials

Characterization of oil-in-water emulsions stabilized by tyrosinase-crosslinked soy glycinin

Partial purification and kinetic characterization of mushroom stem polyphenoloxidase and determination of its storage stability in different lyophilized forms

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