Effect of Trichoderma reesei tyrosinase on rheology and microstructure of acidified milk gels

Ercili-Cura, Dilek; Lille, Martina; Partanen, Riitta; Kruus, Kristiina; Büchert, Johanna; Lantto, Raija

doi:10.1016/j.idairyj.2010.06.008

Cited by 45 publications

(23 citation statements)

References 39 publications

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“…This is especially true for urea-PAGE, which also exploits charge differences for separation (see also [62,75,76]), but also in the case of SDS-PAGE, where whey proteins are also clearly separated from caseins [36,62,77,78]. Therefore, susceptibility of different casein types to particular cross-linking reactions can be easily estimated.…”

Section: Advantages and Limitations In The Context Of Casein Investigmentioning

confidence: 99%

“…In fact, Ikura et al [95] were one of the first using SDS-PAGE to monitor enzymatic casein polymerisation, followed by numerous further studies. For raw milk it was shown that cross-linking with TGase was prevented presumably by an indigenous inhibitor [77,96,97]; however, other authors achieved casein cross-linking in raw milk [78]. Using SDS-PAGE, the cross-linking potential of laccase preparations from different microbial origins [98] as well as the suitability of different reaction-mediating additives [99] were evaluated for application in milk gels.…”

Section: Literature Review Of Studies On Cross-linked Caseinmentioning

confidence: 99%

“…For instance, Tang et al [89] studied the susceptibility of non-micellar sodium caseinate to TGase, but the determined order of κ-casein > α S -casein > β-casein might rather be a result of false band assignments. In spite of studies that have shown an order of β-casein > α S -casein > κ-casein, e.g., [77,78,80], this information is still cited in the literature, e.g., [27,102]. On the other hand, it is generally acknowledged that κ-casein is most susceptible to TGase in case of micellar casein because of high accessibility on the micelle surface, e.g., [78,92,[103][104][105][106][107][108].…”

Section: Literature Review Of Studies On Cross-linked Caseinmentioning

confidence: 99%

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Size Separation Techniques for the Characterisation of Cross-Linked Casein: A Review of Methods and Their Applications

et al. 2018

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Abstract:Casein is the major protein fraction in milk, and its cross-linking has been a topic of scientific interest for many years. Enzymatic cross-linking has huge potential to modify relevant techno-functional properties of casein, whereas non-enzymatic cross-linking occurs naturally during the storage and processing of milk and dairy products. Two size separation techniques were applied for characterisation of these reactions: gel electrophoresis and size exclusion chromatography. This review summarises their separation principles and discusses the outcome of studies on cross-linked casein from the last~20 years. Both methods, however, show limitations concerning separation range and are applied mainly under denaturing and reducing conditions. In contrast, field flow fractionation has a broad separation range and can be easily applied under native conditions. Although this method has become a powerful tool in polymer and nanoparticle analysis and was used in few studies on casein micelles, it has not yet been applied to investigate cross-linked casein. Finally, the principles and requirements for absolute molar mass determination are reviewed, which will be of increased interest in the future since suitable calibration substances for casein polymers are scarce.

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Section: Advantages and Limitations In The Context Of Casein Investigmentioning

confidence: 99%

Section: Literature Review Of Studies On Cross-linked Caseinmentioning

confidence: 99%

Section: Literature Review Of Studies On Cross-linked Caseinmentioning

confidence: 99%

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Size Separation Techniques for the Characterisation of Cross-Linked Casein: A Review of Methods and Their Applications

et al. 2018

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“…Storage modulus (G') and loss tangent (tan δ = G''/G', G'', loss modulus) of the dispersions were recorded. Gelation temperature was assigned to the temperature point at which G' ≥ 1 Pa for the gels (Ercili-Cura et al 2010).…”

Section: Methodsmentioning

confidence: 99%

“…TGase-induced modification is able to form a more homogeneous gel network (Faergemand & Qvist 1997;Ercili-Cura et al 2013), and thus improve water retention (Schorsch et al 2000;Ercili-Cura et al 2013) and texture (Ercili-Cura et al 2010) of protein gels.…”

mentioning

confidence: 99%

Effects of transglutaminase-induced modification in the presence of oligochitosan of 1 kDa on the structure and gelling properties of caseinat

Song¹,

Zhao²

2016

Czech J. Food Sci.

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Milk gels have both traditional and high commercial value within the dairy industry (Schorsch et al. 2000;Siamand et al. 2014). Besides renneting, acidification of milk is the most routine way to form milk protein gels. Acidifying milk using glucono-δ-lactone (GDL) can slowly form structured gel products (Lucey 2004). Two major steps are involved in the formation of the acidified milk gels. In the first step, a collapse of the hairy brush of the casein micelles occurs, and the colloidal calcium and phosphate are then dissolved out of the casein micelle as a result of the protonation of ionised phosphate groups (Gaygadzhiev et al. 2009). Micellar structure is thus profoundly altered but without dissociation. In the second step, at a pH value about 5.0, casein precipitates isoelectrically, or under quiescent conditions it forms rather fragile gels (Lucey 2004). The balance between attractive and repulsive forces within protein molecules results in gel formation (Havea 2006;Rocha et al. 2009). Both intrinsic (e.g. amino acid compositions, molecular weights, hydrophobicity, etc.) and extrinsic (protein concentrations, pH value, temperature, metal ions, and ionic strengths) factors all show impacts on gelation and physiochemical properties of protein gels.During the last years, transglutaminase (TGase, EC 2.3.2.13) has been used to modify proteins via inducing protein cross-linking (between glutamine and lysine residues of the proteins) (Anema & Kruif 2012;Domagała et al. 2015). TGase-induced modification is able to form a more homogeneous gel network (Faergemand & Qvist 1997;Ercili-Cura et al. 2013), and thus improve water retention (Schorsch et al. 2000;Ercili-Cura et al. 2013) and texture (Ercili-Cura et al. 2010) of protein gels. 564Food Technology and Economy, Engineering and Physical Properties Czech J. Food Sci., 34, 2016 (6) Caseinate, transglutaminase (TGase), and an oligochitosan of 1 kDa were used to prepare a glycated and cross-linked caseinate (GC-caseinate), aiming to assess potential changes in both the structure and gelling properties of such caseinate. The results of Fourier transform infrared analysis revealed that only GC-caseinate contained saccharide portions in its molecules, evidencing TGase-induced caseinate glycation. Circular dichroism results showed that GC-caseinate possessed a more ordered secondary structure than caseinate. Other results also demonstrated that TGase-induced modification resulted in a lower gelation temperature of GC-caseinate (59°C vs. 68°C) and increased the final tan δ value (0.30 vs. 0.15) compared to caseinate during the development of acidified gels. In addition, the acidified gels from GC-caseinate were detected to have lower water holding capacity (0.720 vs. 0.781 g/g gels), expanded gel network, and larger pore sizes than those from caseinate. It is thus evidenced that the used TGase-induced modification could confer caseinate with ordered secondary structure, expanded gel network but lower water holding capacity.

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Oxidoreductase enzymes: Characteristics, applications, and challenges as a biocatalyst

Cárdenas‐Moreno,

González‐Bacerio,

García Arellano

et al. 2023

Biotech and App Biochem

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Oxidoreductases are enzymes with distinctive characteristics that favor their use in different areas, such as agriculture, environmental management, medicine, and analytical chemistry. Among these enzymes, oxidases, dehydrogenases, peroxidases, and oxygenases are very interesting. Because their substrate diversity, they can be used in different biocatalytic processes by homogeneous and heterogeneous catalysis. Immobilization of these enzymes has favored their use in the solution of different biotechnological problems, with a notable increase in the study and optimization of this technology in the last years. In this review, the main structural and catalytical features of oxidoreductases, their substrate specificity, immobilization, and usage in biocatalytic processes, such as bioconversion, bioremediation, and biosensors obtainment, are presented.

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Effect of Trichoderma reesei tyrosinase on rheology and microstructure of acidified milk gels

Cited by 45 publications

References 39 publications

Size Separation Techniques for the Characterisation of Cross-Linked Casein: A Review of Methods and Their Applications

Size Separation Techniques for the Characterisation of Cross-Linked Casein: A Review of Methods and Their Applications

Effects of transglutaminase-induced modification in the presence of oligochitosan of 1 kDa on the structure and gelling properties of caseinat

Oxidoreductase enzymes: Characteristics, applications, and challenges as a biocatalyst

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