Chemical interactions and rheological properties of hairtail (Trichiurus haumela) surimi: Effects of chopping and pressure

Chen, Yanting; Xu, Anqi; Yang, Rong; Jia, Ru; Zhang, Jinjie; Xü, Dong; Yang, Wenge

doi:10.1016/j.fbio.2020.100781

Cited by 17 publications

(15 citation statements)

References 44 publications

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“…Then, G′ increased and reached its first peak at 48 °C. At low temperatures, protein interactions occur in the gel and form a preliminary gel network structure through weak bonds [20] . Thereafter, the second low value was reached at about 55 °C and then rose rapidly.…”

Section: Resultsmentioning

confidence: 99%

“…The prepared shrimp surimi gel was cut into cylinders with a length of 2.0 cm and equilibrated at room temperature for 30 min. Gel strength was measured using a texture analyser (TMS-Pro, Food Technology Corporation, USA) equipped with a spherical plunger (P/0.5 S, 12.7 mm diameter) in accordance with the method of Chen et al [20] with some slight modifications. The test conditions were as follows: test speed, 1 mm/s; trigger force, 30 g; displacement, 10 mm.…”

Section: Methodsmentioning

confidence: 99%

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Ultrasonic pretreatment improves the gelation properties of low-salt Penaeus vannamei (Litopenaeus vannamei) surimi

Zhang

Wang

Feng

et al. 2022

Ultrasonics Sonochemistry

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Ultrasonic pretreatment improves the gelation properties of low-salt Penaeus vannamei (Litopenaeus vannamei) surimi

Zhang

Wang

Feng

et al. 2022

Ultrasonics Sonochemistry

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“…Subsequently, the cross-linking of -SH occurred followed by the formation of more disulfide bonds [ 36 ]. Nevertheless, faced with stress from starch, SCG showed minor changes in total sulfhydryl groups, contributing to a more stable structure formed by low-temperature preincubation [ 37 ].…”

Section: Resultsmentioning

confidence: 99%

Changes in Gel Structure and Chemical Interactions of Hypophthalmichthys molitrix Surimi Gels: Effect of Setting Process and Different Starch Addition

Jiang

Chen

Xiao

et al. 2021

Foods

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The modifications of histological properties and chemical forces on heated surimi gels with starch addition (0–12 g/100 g surimi) were investigated. Two types of heating processes (direct heating and two-step heating) were carried out on surimi gels in order to reveal the effect of setting on mixed matrices. The results of transverse relaxation time showed less immobile water and free water converted into bound water in a matrix subjected to the setting process. Scanning electron microscope and light microscopy images revealed inefficient starch-swelling in two-step heated gels. Chemical interactions and forces in direct cooking gels were more vulnerable to starch addition, resulting in significant decreases in hydrophobic interaction and sulfhydryl content (p < 0.05). With the increment of starch, the disulfide stretching vibrations of the gauche–gauche–gauche conformation were reduced in both gel matrices. The structural variations of different components collectively resulted in changes in texture profile analysis and water holding capacity. Overall, the results demonstrated that starch addition had a great and positive effect on the weak gel matrix by direct heating.

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“…The effects of oxidation caused by increasing hydroxyl radicals on myofibrillar protein were expressed by the results in the E64 group, which demonstrated increased and then decreased carbonyl contents, declined total sulfhydryl contents of myofibrillar protein, decreased intensity bands of MHC and actin, decreased ionic bonds, and increased disulfide bonds between the molecular myofibrillar protein. Chen et al [45] suggested that hydrophobic interactions and disulfide bonds are the main chemical interactions for stabilizing the gel structure. In present study, the breaking force and gel strength of E64 gels reached the highest level at 10 mM H 2 O 2 probably because the E64 gels had higher hydrophobic interactions (1.51 mg/mL) and moderate disulfide bonds (0.42 mg/mL) between gel molecules at 10 mM H 2 O 2 .…”

Section: Discussionmentioning

confidence: 99%

Effects of Cathepsins on Gel Strength and Water-Holding Capacity of Myofibrillar Protein Gels from Bighead Carp (Aristichthys nobilis) under a Hydroxyl Radical-Generation Oxidizing System

Han

Liang

Zhang

et al. 2022

Foods

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This study investigates the effects of cathepsins on the gel strength and water-holding capacity (WHC) of myofibrillar protein gels from bighead carp (Aristichthys nobilis) under a hydroxyl radical-generation oxidizing system. The myofibrillar proteins were divided into control group (with cathepsins) and E64 group (without cathepsins). The changes of cathepsin B and cathepsin L activities, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), protein oxidation (total sulfhydryl and carbonyl contents), and chemical interactions (nonspecific association, ionic bonds, hydrogen bonds, hydrophobic interactions, and disulfides) of myofibrillar protein and gels, as well as the gel strength and WHC of two groups under 0–100 mM H2O2, were measured. The results indicated that mild oxidation (10 mM H2O2) made a better gel strength and WHC. Cathepsin B and L activities decreased with increasing H2O2 concentrations but their effects on myofibrillar protein degradation still existed during 0.1–50 mM H2O2, which was expressed by higher carbonyl contents and ionic bonds at 0.1 and 50 mM H2O2, higher total sulfhydryl contents at 0 mM H2O2, and a lower intensity of MHC and actin of the control group than the E64 group. Besides more protein degradation, cathepsin proteolysis also resulted in lower gel strength and WHC in control gels than E64 gels under mild oxidation, which could be explained by lower hydrophobic interaction and moderate disulfides bonds between gel protein molecules of control gels.

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Chemical interactions and rheological properties of hairtail (Trichiurus haumela) surimi: Effects of chopping and pressure

Cited by 17 publications

References 44 publications

Ultrasonic pretreatment improves the gelation properties of low-salt Penaeus vannamei (Litopenaeus vannamei) surimi

Ultrasonic pretreatment improves the gelation properties of low-salt Penaeus vannamei (Litopenaeus vannamei) surimi

Changes in Gel Structure and Chemical Interactions of Hypophthalmichthys molitrix Surimi Gels: Effect of Setting Process and Different Starch Addition

Effects of Cathepsins on Gel Strength and Water-Holding Capacity of Myofibrillar Protein Gels from Bighead Carp (Aristichthys nobilis) under a Hydroxyl Radical-Generation Oxidizing System

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