Properties of bovine gelatin as affected by a cross-linking induced by horseradish peroxidase, glucose oxidase and glucose

Ming, Liao; Han, Yan-Ping; Zhao, Xin‐Huai

doi:10.1007/s11694-017-9686-z

Cited by 2 publications

(3 citation statements)

References 36 publications

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“…37 For example, the casein cross-linked by TGase had lower EAI but higher ESI values, 38,39 whereas the bovine gelatin cross-linked by HRP, glucose oxidase, and D-glucose also had reduced EAI but increased ESI. 14 From a chemical point of view, protein polymers of larger molecular weights have extended structures, which hinders their interfacial absorption and denaturation. 40,41 Thus, the cross-linked proteins mostly were observed with lower emulsifying activity than the unmodified proteins.…”

Section: Water-/oil-binding and Emulsification Changes In Response Tomentioning

confidence: 99%

“…11 Moreover, a ternary system comprising the three elements horseradish peroxidase (HRP; EC 1.11.1.7), glucose oxidase (EC 1.1.3.4) and D-glucose was also used to induce the crosslinking of several proteins like SPI, caseinate and gelatin. [12][13][14] Theoretically, glucose oxidase catalyzes D-glucose oxidation to form H 2 O 2 and D-glucono-⊐-lactone (GDL). HRP thus can utilize H 2 O 2 as a reactant to catalyze dityrosine formation in proteins, which leads to altered molecular structures and a change in protein properties.…”

Section: Introductionmentioning

confidence: 99%

“…When caseinate was cross‐linked and glucosamine‐conjugated under the action of TGase, its emulsifying, foaming and rheological properties were improved 11 . Moreover, a ternary system comprising the three elements horseradish peroxidase (HRP; EC 1.11.1.7), glucose oxidase (EC 1.1.3.4) and D‐glucose was also used to induce the cross‐linking of several proteins like SPI, caseinate and gelatin 12–14 . Theoretically, glucose oxidase catalyzes d ‐glucose oxidation to form H 2 O 2 and d ‐glucono‐δ‐lactone (GDL).…”

Section: Introductionmentioning

confidence: 99%

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Property changes of caseinate in response to its dityrosine formation induced by horseradish peroxidase, glucose oxidase and d‐glucose

Chang

et al. 2020

J Sci Food Agric

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BACKGROUND: A ternary system containing horseradish peroxidase (HRP), glucose oxidase and D-glucose using one-or twostep treatment was evidently able to cross-link proteins via dityrosine formation and thus was assessed for its possible impact on several properties of a protein ingredient caseinate. RESULTS: HRP, glucose oxidase and D-glucose were used at 200 U, 6 U and 0.05 mmol g −1 protein to treat caseinate by one-and two-step methods, producing two cross-linked caseinates named CLCN-I and CLCN-II, respectively. In response to the conducted cross-linking, both CLCN-I and CLCN-II gained slightly reduced dispersibility at pH 5-10, enlarged hydrodynamic radius (particle size distribution, 266.37 and 258.33 versus 226.67 nm) and negative zeta-potential (−26.60 and −22.27 versus −14.30 mV) in dispersions, increased water-binding (3.70 and 3.09 versus 2.68 kg kg −1 protein), decreased oil-binding (1.75 and 2.74 versus 2.87 kg kg −1 protein) and emulsifying activity (76.2 and 82.3 versus 94.3 m 2 g −1 protein), increased emulsion stability (84.3% and 82.5% versus 78.6%), and enhanced thermal stability with lower mass loss (58.5% and 59.6% versus 64.3%) or higher decomposition temperatures (331.2°C and 328.7°C versus 327.6°C) upon heating at 105-450°C. In addition, CLCN-I and CLCN-II had decreased gelling temperatures and shortened gelling times when forming acid-induced gels, and the gels were endowed with increased values in four textural indices and finer microstructure. Moreover, CLCN-I with a higher cross-linking extent showed greater property changes than CLCN-II. CONCLUSION: This ternary system could be used in caseinate cross-linking to improve properties such as aggregation, emulsification, gelation and thermal stability.

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Section: Water-/oil-binding and Emulsification Changes In Response Tomentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Property changes of caseinate in response to its dityrosine formation induced by horseradish peroxidase, glucose oxidase and d‐glucose

Chang

et al. 2020

J Sci Food Agric

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Investigation of average crosslink distance and physicochemical properties of gummy candy during storage: Effect of formulation and storage temperature

2023

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Texture is linked to food structure at micro- and macro-levels. The most effective way to manipulate gel texture is to change the number of crosslinks per unit volume. Polymer concentration and type can be changed or the amount of evaporated water can be adjusted to achieve this. Gummy candy is a good food model to investigate texture due to the presence of versatile polymer gelling agents. The estimation of average cross-link distance is a good approach to monitor candy texture. Physicochemical properties are useful indicators showing storage stability. In this study, gummy candies were prepared with different glucose sirup:sucrose ratios (1.1 and 1.5), starch (0% and 1.5%), and gelatin (3% and 6%) concentrations. Texture (hardness), moisture content, water activity (aw), total soluble solids (TSS), and pH were measured. Candies were stored at 10, 20, and 30 °C for 12 weeks and at ambient temperatures of 15–22 °C for 52 weeks. Gelatin concentration, moisture content, storage time, and temperature affected hardness. At 1.5 glucose sirup:sucrose ratio, average cross-link distance decreased after 10 °C storage for 3% gelatin level and it increased after 20 and 30 °C storage for 6% gelatin and 0% starch level; however, it did not change for 15–22 °C storage. Moisture content, aw, TSS, and pH were affected by glucose sirup:sucrose ratio. A Weibullian model was used to express quality changes, and physicochemical indicators did not have an integer kinetic order. Tracking of physicochemical properties and texture with average cross-link distance calculation and modeling is useful for storage stability studies showing the quality of food gel products.

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Properties of bovine gelatin as affected by a cross-linking induced by horseradish peroxidase, glucose oxidase and glucose

Cited by 2 publications

References 36 publications

Property changes of caseinate in response to its dityrosine formation induced by horseradish peroxidase, glucose oxidase and d‐glucose

Property changes of caseinate in response to its dityrosine formation induced by horseradish peroxidase, glucose oxidase and d‐glucose

Investigation of average crosslink distance and physicochemical properties of gummy candy during storage: Effect of formulation and storage temperature

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