Disruption of secondary structure by oxidative stress alters the cross-linking pattern of myosin by microbial transglutaminase

Li, Chunqiang; Xiong, Youling L.

doi:10.1016/j.meatsci.2015.05.024

Cited by 50 publications

(16 citation statements)

References 35 publications

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“…These imply that mild oxidation enhanced the cross‐linking of MHC by MTG but excessive oxidation inhibited the action. Similar result was reported by Li and Xiong (), who found that mild oxidation (0.1–1 mM H 2 O 2 ) promoted MTG‐mediated cross‐linking while strong oxidation (5–20 mM H 2 O 2 ) decreased MTG efficiency in porcine MFP. Rheological analysis showed that G ′ of MFP oxidized by 1 mM H 2 O 2 was the highest but G ′ of MFP oxidized by 16 mM H 2 O 2 was the lowest (Figure b), in agreement with the results of SDS‐PAGE electrophoresis.…”

Section: Resultssupporting

confidence: 89%

“…Rheological analysis showed that G ′ of MFP oxidized by 1 mM H 2 O 2 was the highest but G ′ of MFP oxidized by 16 mM H 2 O 2 was the lowest (Figure b), in agreement with the results of SDS‐PAGE electrophoresis. It is hypothesized that mild oxidation induced unfolding of helical structure, enabling cross‐linking of all fragments of myosin by MTG (Li & Xiong, ). This also changed the cross‐linking pattern led by MTG and promoted its effects.…”

Section: Resultsmentioning

confidence: 99%

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Physiochemical and rheological properties of oxidized Japanese seerfish (Scomberomorus niphonius) myofibrillar protein

et al. 2019

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Myofibrillar protein (MFP) of Japanese seerfish (JS) was oxidized by Fenton system (1, 4, 8, 16 mM H2O2 for 0, 2, 4, 6 hr). After oxidation, α‐helix ratio and sulfhydryl content of MFP declined along with the increased carbonyl and dityrosine levels. Bromophenol blue bound in MFP under 1 mM H2O2 slightly increased. Polymers together with attenuated myosin heavy chain in protein pattern were observed. Compared with non‐oxidized MFP, storage modulus (G′) of MFP subjected to 1 mM H2O2 for 4 hr increased while that of MFP exposed to 16 mM H2O2 declined. When treated with microbial transglutaminase (MTG), mildly oxidized (1 mM H2O2, 2 hr) MFP showed higher G′ while heavily oxidized (16 mM H2O2, 2 hr) MFP had lower G′ than control. Oxidation showed pronounced influences on physiochemical and gelling properties of JS MFP and the oxidation extent affected MTG role on it. Practical applications Protein oxidation occurs extensively in muscle and exerts great influences on muscle food quality. JS is widely used for producing gel food in China. Its muscle also contains oxidation initiators such as H2O2, hemoglobin and lipids, increasing the susceptibility to protein oxidation. Results of the study exposed the effects of hydroxyl radical oxidation on physiochemical and gelling properties of JS MFP. It provides strategic support to improve gel properties of MFP by manipulating oxidation.

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Section: Resultssupporting

confidence: 89%

Section: Resultsmentioning

confidence: 99%

Physiochemical and rheological properties of oxidized Japanese seerfish (Scomberomorus niphonius) myofibrillar protein

et al. 2019

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“…In addition, cross linkers can transform some structural properties of macromolecules and create covalent bonds between biopolymers or matrices (Buchert et al ., ). Biological enzymatic crosslinking, with its nontoxic, feasible and efficient properties, is considered to be the most ideal candidate for cross‐linking materials (Li & Xiong, ). Transglutaminase (TG, EC 2.3.2.13, TGase) from microorganisms has been extensively applied to promote protein crosslinking by catalysing acyl transfer reactions to improve food protein functionality (Stachel et al ., ).…”

Section: Introductionmentioning

confidence: 99%

Influence of natamycin loading on the performance of transglutaminase‐induced crosslinked gelatin composite films

Liu

Qian

et al. 2019

Int J of Food Sci Tech

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Summary We investigated the effect of natamycin on the physicochemical properties of crosslinked gelatin films. Natamycin decreased the tensile strength, elongation at break and water vapour barrier of crosslinked gelatin films. The thermal stability of the crosslinked gelatin films varied considerably with natamycin amount. The crosslinked films gradually turned yellow‐green in colour with increasing natamycin content. The aforementioned different influences were associated with the altered microstructure and crystallinity of the crosslinked films induced by increasing natamycin amounts. The performance changes in the films could be attributed to the increase in natamycin, resulting in enhanced natamycin crystallinity, which was confirmed by X‐ray diffraction and Fourier transform infrared spectroscopy. Moreover, the crosslinking reaction could confer resistance to damage in TGase‐induced aggregation caused by natamycin crystallinity. Therefore, the findings in this paper will facilitate the development of gelatin‐based food‐contact film materials and provide theoretical direction for the packing industry.

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“…This result is consistent with previous studies; Batra et al reported that modification of the OVA ɛ‐amino groups resulted in a substantial decrease in α‐helix (Batra, Roebuck, & Uetrecht, ). Furthermore, Li et al found that the helical structure of myofibrillar protein was unraveled by oxidation (Li & Xiong, ).…”

Section: Resultsmentioning

confidence: 99%

Effect of hydroxyl radical-induced oxidation on the structure and heat-induced gel properties of ovalbumin

Geng

Huang

et al. 2018

J Food Process Preserv

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The present study is aimed to investigate the effect of hydroxyl radical‐induced oxidation on the structure and gel properties of chicken ovalbumin. With the increase in oxidation time and H2O2 dose, the carbonyl content in ovalbumin increased, while the free sulfhydryl content decreased. The effect of oxidation on the structure of ovalbumin was examined, and the results indicated that the disorder level increased. Oxidation of ovalbumin lowered the solubility, and the viscosity of the solution decreased significantly. Oxidation weakened the water holding capacity and gel hardness, as well as resulting in significant changes in the microstructure of ovalbumin gels. Hydroxyl radical‐induced oxidation caused destabilization of the ovalbumin structure, thereby affecting the heat‐induced gel properties. Practical applications The present study demonstrated the effect of hydroxyl radical‐induced oxidation on chicken OVA, concluding that the oxidation might be one of the primary reasons for the degradation of its gel properties. Consequently, avoiding protein oxidation during storage and processing would help maintain the functional properties of the chicken egg white. Therefore, this study provides important information for the research and application of ovalbumin.

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Disruption of secondary structure by oxidative stress alters the cross-linking pattern of myosin by microbial transglutaminase

Cited by 50 publications

References 35 publications

Physiochemical and rheological properties of oxidized Japanese seerfish (Scomberomorus niphonius) myofibrillar protein

Physiochemical and rheological properties of oxidized Japanese seerfish (Scomberomorus niphonius) myofibrillar protein

Influence of natamycin loading on the performance of transglutaminase‐induced crosslinked gelatin composite films

Effect of hydroxyl radical-induced oxidation on the structure and heat-induced gel properties of ovalbumin

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