Effects of apple polyphenols and hydroxypropyl-β-cyclodextrin inclusion complexes on the oxidation of myofibrillar proteins and microstructures in lamb during frozen storage

Zhong, Yuanyuan; Han, Ping-Hsuan; Sun, Suling; An, Ning; Ren, Xudong; Lü, Shiling; Wang, Qingling; Dong, Jun

doi:10.1016/j.foodchem.2021.131874

Cited by 26 publications

(8 citation statements)

References 43 publications

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“…4 A). The CD spectrum of MPs displayed two negative bands corresponding to the α-helix structure near 208 and 222 nm, reflecting the predominance of the α-helix structure of myosin rods [33] . Obviously, the intense negative troughs of each of these two peaks were present in the native MPs, due to the superhelix conformation formed by the aggregation of myosin rods, and indicating the presence of many myosin filaments in the aqueous MP suspension [6] .…”

Section: Resultsmentioning

confidence: 99%

Improved water solubility of myofibrillar proteins by ultrasound combined with glycation: A study of myosin molecular behavior

Han

Liu

et al. 2022

Ultrasonics Sonochemistry

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Section: Resultsmentioning

confidence: 99%

Improved water solubility of myofibrillar proteins by ultrasound combined with glycation: A study of myosin molecular behavior

Han

Liu

et al. 2022

Ultrasonics Sonochemistry

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“…This is supported by decreased sulfhydryl content and Ca 2+ ‐ATPase activity. In addition, the increase of particle size demonstrated that oxidation destroyed the delicate equilibrium between proteins' non‐covalent interactions, leading to protein denaturation and aggregation (Zhong et al ., 2022). At the same time, the MPs treated with ClO 2 + SAEW displayed less pronounced increases in particle size than that of CK group, which indicated that ClO 2 + SAEW effectively inhibited protein oxidation.…”

Section: Resultsmentioning

confidence: 99%

Stable chlorine dioxide combined with slightly acidic electrolyzed water: an effective way to delay protein deterioration of refrigerated large yellow croaker (Pseudosciaena crocea)

Lan,

Zhou,

Zhao

et al. 2023

Int J of Food Sci Tech

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SummaryFish is susceptible to spoilage for enzymatic and microbial activities during storage, proteolysis of MPs by endogenous proteases played a crucial influence in the early postmortem decomposition of myosin. This study aimed to investigate the impact of stable chlorine dioxide (ClO2) combined with slightly acidic electrolyzed water (SAEW) on myofibrillar proteins (MPs) and endogenous proteases alterations in large yellow croaker (Pseudosciaena crocea) during cold storage. The results of Fourier‐transform infrared spectroscopy (FT‐IR) and intrinsic fluorescence intensity (IFI) showed that the ClO2 + SAEW treatment kept the structural stability of protein in fillets during cold storage. Moreover, ClO2 + SAEW treatment dramatically inhibited protein degradation and oxidation. The results of light microscopy further confirmed the results. Meanwhile, there was a tendency to first increase and then decrease on the activities of calpain and cathepsin B, L. According to the correlation analysis and principal component analysis, the activities of endogenous proteases (cathepsin B, D, L, and calpain) were significant (P<0.01) positively correlated to MFI and TCA‐soluble peptide, and were significant (P<0.01) negative correlated with the contents of total sulfhydryl and Ca2+‐ATPase. The endogenous proteases activities and protein deterioration were strongly associated. Therefore, endogenous protease was affected by ClO2 and SAEW, which delayed protein degradation in large yellow croaker, especially ClO2 combined with SAEW treatment.

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“…Three samples ( n = 3) were separated for the initial analysis of fresh meat. Microcapsules were prepared as described in our previous studies, [ 17 ] by mixing APs and hydroxypropyl-β-cyclodextrin in at the mass concentration of 1:1 via freeze drying in the laboratory (the highest encapsulation efficiency of 82.31% and the highest polyphenol loading rate of 46.87% were reached under this condition), obtaining the solutions S1, S2, S3, and S4 with concentrations of 0.2, 0.8, 1.6, and 3.2 mg/mL, respectively. The remaining samples ( n = 75) were randomly divided into 5 groups: Group 1 received no treatment (control), whereas Groups 2–5 were soaked in MAP solutions of S1, S2, S3, and S4 for 60 min (4 °C) and then drip dried in a stainless-steel orifice plate (5 min).…”

Section: Methodsmentioning

confidence: 99%

Improving the Quality of Frozen Lamb by Microencapsulated Apple Polyphenols: Effects on Cathepsin Activity, Texture, and Protein Oxidation Stability

Zhong

Liu

et al. 2022

Foods

Self Cite

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This study aimed to evaluate the efficiency of microencapsulated apple polyphenols (MAP) in controlling cathepsin activity and texture, as well as inhibiting protein oxidation and metmyoglobin formation in lamb meat during frozen storage at −18 °C for 40 weeks. The effects of degradation in vitro on cathepsin and the microstructure in lamb were also evaluated. Results indicated that relative to the control group, the lamb treated with MAP exhibited increased cathepsin activity and inhibited metmyoglobin production. Textural characteristics, such as hardness and springiness, significantly changed (p < 0.05). Treatment with 0.2–1.6 mg/mL of MAP effectively reduced the mean particle size, increasing the zeta potential, delaying the conversion of α-helices to random coils, and maintaining the integrity of the tissue structure. However, treatment with 3.2 mg/mL of MAP damaged the protein structure. Degradation in vitro indicated that protein oxidation hindered the effect of cathepsin and was a dominant factor affecting protein during the frozen storage. These results demonstrated that microencapsulation can potentially be used for meat preservation and replace chemical antioxidants in the meat industry.

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Effects of apple polyphenols and hydroxypropyl-β-cyclodextrin inclusion complexes on the oxidation of myofibrillar proteins and microstructures in lamb during frozen storage

Cited by 26 publications

References 43 publications

Improved water solubility of myofibrillar proteins by ultrasound combined with glycation: A study of myosin molecular behavior

Improved water solubility of myofibrillar proteins by ultrasound combined with glycation: A study of myosin molecular behavior

Stable chlorine dioxide combined with slightly acidic electrolyzed water: an effective way to delay protein deterioration of refrigerated large yellow croaker (Pseudosciaena crocea)

Improving the Quality of Frozen Lamb by Microencapsulated Apple Polyphenols: Effects on Cathepsin Activity, Texture, and Protein Oxidation Stability

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