Natural product procyanidin B1 as an antitumor drug for effective therapy of colon cancer.

Traditional chemotherapy drugs have definite antitumor mechanisms and good therapeutic efficacy; however, their poor water solubility, serious side effects and drug resistance limit their clinical application. To the best of our knowledge, the present study reported for the first time the in vivo and in vitro anticancer effects of procyanidin B1 (PCB1), a compound that is isolated from natural sources such as grape seeds, apples, peanut skin and cranberries. Cell Counting Kit-8 assay showed that PCB1 effectively decreased the number of viable HCT-116 cells compared with cells treated with the small molecule cytotoxic drug doxorubicin. Quantitative PCR and apoptosis analysis, Cell cycle analysis, and WB analysis) of the molecular mechanism showed that PCB1 induced cell apoptosis and cell cycle arrest in S phase by increasing expression of pro-apoptosis protein caspase-3 and BAX and decreasing expression of anti-apoptosis protein Bcl-2. The efficient antitumor activity of PCB1 was demonstrated through in vivo experiments on a xenograft mouse model, demonstrating that PCB1 significantly suppressed tumor growth. The present study suggested that PCB1 represents a novel class of plant-based compounds isolated from natural sources that can be applied as an anticancer drug.

Dynamic Changes of the Microbial Community and Volatile Organic Compounds of the Northern Pike (Esox lucius) during Storage.

In this study, the quality (sensory evaluation, microbial enumerate, color, tvb-n (total volatile basic nitrogen), tca-soluble peptide (trichloroacetic acid-soluble peptide), muscle glucose, lactate, total sugar, Bas (Biogenic amines), VOCs (volatile organic compounds) and the microbial dynamic structure in samples stored at 4 °C were evaluated, and the relationship between VOCs and the diversity structure of microorganisms was also discussed. It was determined by sensory evaluation that the shelf life of samples was around 8 days. Protein and sugar were detected in large quantities by microorganisms in the later stage. At the same time, this also caused a large amount of Bas (biogenic amines) (tyramine, cadaverine, and putrescine). According to high-throughput amplicon sequencing, the initial microbiota of samples was mainly composed of Pseudomonas, Acinetobacter, Planifilum, Vagococcus, Hafnia, Mycobacterium, Thauera, and Yersinia. Among them, Pseudomonas was the most advantageous taxon of samples at the end of the shelf life. The minor fraction of the microbial consortium consisting of Vagococcus, Acinetobacter and Myroides was detected. The substances 3-methyl-1-butanol, ethyl acetate, and acetone were the main volatile components. The glucose, lactic acid, and total sugar were negatively correlated with Yersinia, Hafnia-Obesumbacterium, Thauera, Mycobacterium, and Planifilum; the proportion of these microorganisms was relatively high in the early stage. TVB-N and TCA-soluble peptides were positively correlated with Pseudomonas, Shewanella, Brochothrix, Vagococcus, Myroides, and Acinetobacter, and these microorganisms increased greatly in the later stage. The substance 3-methyl-1-butanol was positively correlated with Pseudomonas and negatively correlated with Mycobacterium. Ethyl acetate was associated with Hafnia-Obesumbacterium, Thauera, and Yersinia. Acetone was positively correlated with Acinetobacter.

Effects of CaCl2 on 3D Printing Quality of Low-Salt Surimi Gel.

In order to develop low-salt and healthy surimi products, we limited the amount of NaCl to 0.5 g/100 g in this work and studied the effect of CaCl2 (0, 0.5, 1.0, 1.5, and 2.0 g/100 g) on the 3D printing quality of low-salt surimi gel. The results of rheology and the 3D printing showed that the surimi gel with 1.5 g/100 g of CaCl2 added could squeeze smoothly from the nozzle and had good self-support and stability. The results of the chemical structure, chemical interaction, water distribution, and microstructure showed that adding 1.5 g/100 g of CaCl2 could enhance the water-holding capacity and mechanical strength (the gel strength, hardness, springiness, etc.) by forming an orderly and uniform three-dimensional network structure, which limited the mobility of the water and promoted the formation of hydrogen bonds. In this study, we successfully replaced part of the salt in surimi with CaCl2 and obtained a low-salt 3D product with good printing performance and sensory properties, which could provide theoretical support for the development of healthy and nutritious surimi products.

The Effects of Malonaldehyde on Quality Characteristics and Protein Oxidation of Coregonus peled (Coregonuspeled) during Storage.

The effects of changes in the malondialdehyde (MDA) content on the quality of fish during the low-temperature storage period are unclear. Therefore, the effects of the MDA content on Coregonus peled quality and protein changes were investigated following storage under refrigeration (4 °C) and super chilling (-3 °C) for 15 days (d). The results showed that the MDA content continued to increase during storage and that the highest content was produced at 1.42 mg/kg during refrigeration. The fillet pH, drip loss, texture (hardness and elasticity), and myofibril fragmentation index deteriorated significantly during the storage period. Increased oxidation of the myofibrillar protein (MP) was observed in the 15 d storage period, and the MP carbonyl content was 1.19 times higher under refrigeration than in super chilling, while the protein α-helix structure decreased by 12.48% and 12.20% under refrigeration and super chilling, respectively. Electropherograms also showed that myosin degradation was particularly severe in the refrigeration storage period of 15 d. Overall, the MDA formed at the refrigeration and super chilling storage temperatures could promote structural changes in, and the oxidative degradation of, proteins to different degrees, leading to the deterioration of the fillet quality. This study provides a scientific basis for investigating the relationship between fish quality and changes in the MDA content during low-temperature storage.

Effects of oxidation on the physicochemical properties and degradation of mutton myofibrillar proteins.

Tenderness affects mutton quality and price, and the degradation of myofibrillar protein (MP) is critical to improve tenderness. We investigated the oxidative modification of mutton MP by hydroxyl radicals (OH) and the effects of this modification on the proteolysis of MP by µ-calpain. As the H2 O2 concentrations increased, the carbonyl and dityrosine contents and the surface hydrophobicity of MP all display an increasing trend, whereas the total sulfhydryl and intrinsic fluorescence intensity of MP declines significantly. SDS-PAGE electrophoresis indicates that disulfide bonds and other covalent bonds led to protein cross-linking and aggregation. After adding µ-calpain, with increasing oxidation, the degradation percentage of myosin heavy chain (MHC) increases considerably and actin degradation is promoted, while the proteolysis of troponin-T and desmin is inhibited. These data suggest that·OH can change MP physicochemical properties and its susceptibility to µ-calpain. Future investigations will focus on the effect of oxidation on the degradation of MP by other proteases, such as cathepsins and caspase and the effect of oxidation on these enzymes. PRACTICAL APPLICATION: The calpain system, particularly µ-calpain, plays a pivotal role in postmortem tenderization of meat. Protein oxidative modifications influence meat tenderness mainly by regulating proteolysis. An investigation of the effect of oxidation on the proteolytic susceptibility of MP to degradation by µ-calpain allows for the monitoring of the association between protein oxidation and meat tenderness.

Effects of Ultrasonic Treatment on the Structure, Functional Properties of Chickpea Protein Isolate and Its Digestibility In Vitro.

This study evaluated the effects of different levels of ultrasonic power (200, 400, 600 W) and treatment time (0, 10, 15 and 30 min) on the structure, emulsification characteristics, and in vitro digestibility of chickpea protein isolate (CPI). The changes in surface hydrophobicity of CPI indicated that ultrasound treatment exposed more hydrophobic amino acid residues. The analysis of sulfhydryl content and zeta potential showed that ultrasound caused the disulfide bond of CPI to be opened, releasing more negatively charged groups, and the solution was more stable. In addition, Fourier Transform Infrared Spectroscopy (FT-IR) and intrinsic fluorescence spectroscopy showed that ultrasound changes the secondary and tertiary structure of CPI, which is due to molecular expansion and stretching, exposing internal hydrophobic groups. The emulsification and foaming stability of CPI were significantly improved after ultrasonic treatment. Ultrasonic treatment had a minor effect on the solubility, foaming capacity and in vitro digestibility of CPI. All the results revealed that the ultrasound was a promising way to improve the functional properties of CPI.

Ultrasonic structural modification of myofibrillar proteins from Coregonus peled improves emulsification properties.

This study evaluated the effects of high intensity ultrasonication (HIU, 100, 150, 200, and 250 W) and treatment time (0, 3, 6, 9, and 12 min) on the structure and emulsification properties of myofibrillar proteins (MPs) from Coregonus peled. These investigations were conducted using an ultrasonic generator at a frequency of 20 kHz (ultrasonic probe). Analysis of the carbonyl content and total number of sulfhydryl groups showed that HIU significantly improved the oxidative modification of MPs (P < 0.05). SDS-PAGE profiling showed significant degradation of the myosin heavy chain (P < 0.05). In addition, Fourier transformed infrared spectroscopy (FTIR) revealed that HIU altered these treated MP secondary structures, this was due to molecular unfolding and stretching, exposing interior hydrophobic groups. Particle size analysis showed that HIU treatment reduced particle sizes. Solubility, emulsification capacity, and emulsion stability were improved significantly, and each decreased with an increase in treatment time (up to 12 min), indicating aggregation with prolonged sonication. These results indicate that HIU could improve the emulsification properties of MPs from C. peled, demonstrating a promising method for fish protein processing.

Effects of µ-calpain oxidation on Coregonus peled myofibrillar protein degradation in vitro.

The aim of this study was to evaluate the effect of µ-calpain oxidation on Coregonus peled myofibrillar protein degradation. In the present study, a hydroxyl radical oxidation system was selected to investigate oxidative modification on µ-calpain activity and its degradation on C. peled myofibrillar protein. When subjected to oxidation, the carbonyl content of µ-calpain significantly increased with the increasing of oxidation levels, and oxidation modification promoted the µ-calpain activity. Incubation of C. peled myofibrillar protein with oxidized µ-calpain resulted in the enhanced degradation of myosin heavy chains, actin, and troponin T, but the degradation of desmin at higher levels of oxidation was slightly inhibited, based on sodium dodecyl sulfate polyacrylamide gel electrophoresis and western blotting. This study suggests that oxidation treatment of µ-calpain could accelerate myofibrillar proteolysis through regulating the enzyme activity during postmortem aging. PRACTICAL APPLICATION: Endogenous proteases, especially µ-calpain, are reported to be involved in fish softening during early postmortem storage, which is critical to muscle quality. The cysteine residues of proteins are particularly sensitive to oxidation. The investigation of the effect of oxidation on µ-calpain (a cysteine protease) activity allows for the monitoring of its role in the postmortem proteolysis of fish myofibrils and the associated softening of fish meat, in an attempt to minimize this softening.

Biochemical changes of Coregonus peled myofibrillar proteins isolates as affected by HRGS oxidation system.

The objective of the study was to research the effect of protein oxidation on the biochemical properties of Coregonus peled muscle proteins. Myofibrillar proteins (MP) prepared from C. peled back muscle was oxidized using a hydroxyl radical-generating system (HRGS: 0.1 mM FeCl3 , 0.1 mM ascorbic acid (Asc) and 1-20 mM H2 O2 ). In the HRGS oxidizing system, the carbonyls, dityrosine content, and the surface hydrophobicity of C. peled MP (p < 0.05) increased with the increasing of H2 O2 concentration and oxidation time, while the total sulfhydryl, free amino groups and the Ca-ATPase activity decreased (p < 0.05). The sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) pattern reflected the formation of protein polymers and protein degradation. The results indicate that protein oxidation and the increasing levels of biochemical alterations of C. peled MP have influence on the quality of C. peled muscle protein. PRACTICAL APPLICATIONS: Protein oxidation plays a major role in the meat quality deterioration of C. peled, which always leads to a change in protein physical and chemical properties. In this study, the biochemical change of MP isolates as affected by HRGS oxidation system was proposed. Such chemical modification leads to loss of protein amino groups, shift in the isoelectric point of the protein, loss of solubility and functionality. Additionally, protein carbonyls have been found to be potentially toxic to humans, and relevant measurement of dityrosine as those have been found to cause health problems after oral administration. So such modifications are of technological and nutritional relevance.

The Discovery of Proteins Associated with Freshness of Coregonus Peled Muscle During Refrigerated Storage.

The aim of this study is to identify the protein indicator of freshness of Coregonus peled using two-dimensional gel electrophoresis (2-DE) and matrix-assisted laser desorption ionization-time-of-flight/time-of-flight mass spectrometry (MALDI-TOF/TOF MS) methods. Samples were obtained prior to (control group) and 2, 4, 6, and 8 days after refrigerated storage for quality and proteomics analysis. Three proteins were found to have significant differential abundance in sample groups during the refrigerated storage, including l-lactate dehydrogenase, adenylate kinase isoenzyme 1, and myosin heavy chain, which were associated with freshness changes of C. peled. The freshness of C. peled fish during the refrigerated storage can be differentiated from the comparison of the specific proteins. PRACTICAL APPLICATION: The changes of food quality pose not only the relative economical loses but also the potential implications on consumer's health. Proteomics can represent a powerful tool to explore potential biomarkers that may be related to meat quality defects. The identification of key protein biomarkers linked to freshness of Coregonus peled allows to monitor the response of the food matrix during storage and try to minimizes these defects.