ABSTRACT
Freeze-drying is a preservation method known for its effectiveness in dehydrating food products while minimizing their deterioration. However, protein denaturation and oxidation during freezing and drying can degrade the quality of meat and aquatic products. Therefore, finding the strategies to ensure the dried products' sensory, functional, and nutritional attributes is crucial. This study aimed to summarize protein denaturation mechanisms and overall quality changes in meat and aquatic products during freezing and drying, while also exploring methods for quality control. Different freeze-drying conditions result in varying levels of oxidation and functionality in meat and aquatic products, leading to changes in quality, such as altered fatty and amino acid compositions, protein digestibility, and sensory attributes. To obtain high-quality dried products by freeze-drying, several parameters should be considered, including sample type, freezing and drying temperatures, moisture content, pulverization effects, and storage conditions.
Subject(s)
Food Preservation , Freeze Drying , Animals , Food Preservation/methods , Quality Control , Meat/analysis , Meat Products/analysis , Seafood/analysis , Protein Denaturation , Oxidation-Reduction , Food HandlingABSTRACT
Existing reviews address bioactive peptides of meat proteins; however, comprehensive reviews summarizing the released sequences and their corresponding parent meat proteins in the digesta are limited. This review explores the bioactive peptides released during the in vitro gastrointestinal (GI) digestion of meat, connecting with parent proteins. The primary bioactivities of meat-derived peptides include angiotensin-converting enzyme (ACE) and dipeptidyl peptidase (DPP)-IV inhibition and antioxidant effects. Myofibrillar, sarcoplasmic, and stromal proteins play a significant role in peptide release during digestion. The release of bioactive peptides varies according to the parent protein and cryptides had short chains, non-toxicity, and great bioavailability and GI absorption scores. Moreover, the structural stability and bioactivities of peptides can be influenced by the digestive properties and amino acid composition of parent proteins. Investigating the properties and origins of bioactive peptides provides insights for enhancing the nutritional quality of meat and understanding its potential health benefits.
Subject(s)
Digestion , Meat Products , Meat , Peptides , Peptides/chemistry , Peptides/metabolism , Animals , Meat Products/analysis , Humans , Meat/analysis , Meat Proteins/chemistry , Meat Proteins/metabolism , Gastrointestinal Tract/metabolismABSTRACT
BACKGROUND/AIM: Macropinocytosis is a non-selective form of endocytosis that facilitates the uptake of extracellular substances, such as nutrients and macromolecules, into the cells. In KRAS-driven cancers, including pancreatic ductal adenocarcinoma, macropinocytosis and subsequent lysosomal utilization are known to be enhanced to overcome metabolic stress. In this study, we investigated the role of Casein Kinase 2 (CK2) inhibition in macropinocytosis and subsequent metabolic processes in KRAS mutant cholangiocarcinoma (CCA) cell lines. MATERIALS AND METHODS: The bovine serum albumin (BSA) uptake indicating macropinocytosis was performed by flow cytometry using the HuCCT1 KRAS mutant CCA cell line. To validate macropinosome, the Rab7 and LAMP2 were labeled and analyzed via immunocytochemistry and western blot. The CX-4945 (Silmitasertib), CK2 inhibitor, was used to investigate the role of CK2 in macropinocytosis and subsequent lysosomal metabolism. RESULTS: The TFK-1, a KRAS wild-type CCA cell line, showed only apoptotic morphological changes. However, the HuCCT1 cell line showed macropinocytosis. Although CX-4945 induced morphological changes accompanied by the accumulation of intracellular vacuoles and cell death, the level of macropinocytosis did not change. These intracellular vacuoles were identified as late macropinosomes, representing Rab7+ vesicles before fusion with lysosomes. In addition, CX-4945 suppressed LAMP2 expression following the inhibition of the Akt-mTOR signaling pathway, which interrupts mature macropinosome and lysosomal metabolic utilization. CONCLUSION: Macropinocytosis is used as an energy source in the KRAS mutant CCA cell line HuCCT1. The inhibition of CK2 by CX-4945 leads to cell death in HuCCT1 cells through alteration of the lysosome-dependent metabolism.
Subject(s)
Bile Duct Neoplasms , Casein Kinase II , Cholangiocarcinoma , Lysosomes , Mutation , Naphthyridines , Phenazines , Pinocytosis , Piperazines , Proto-Oncogene Proteins p21(ras) , Humans , Lysosomes/metabolism , Cell Line, Tumor , Cholangiocarcinoma/pathology , Cholangiocarcinoma/metabolism , Cholangiocarcinoma/genetics , Pinocytosis/drug effects , Proto-Oncogene Proteins p21(ras)/genetics , Proto-Oncogene Proteins p21(ras)/metabolism , Casein Kinase II/metabolism , Casein Kinase II/genetics , Casein Kinase II/antagonists & inhibitors , Piperazines/pharmacology , Bile Duct Neoplasms/pathology , Bile Duct Neoplasms/metabolism , Bile Duct Neoplasms/genetics , rab7 GTP-Binding Proteins/metabolism , Cell Death/drug effects , Apoptosis/drug effects , Lysosomal-Associated Membrane Protein 2/metabolism , Lysosomal-Associated Membrane Protein 2/genetics , rab GTP-Binding Proteins/metabolism , rab GTP-Binding Proteins/geneticsABSTRACT
This study investigated whether the freezing-then-aging treatment of beef affects protein digestibility and release of potentially bioactive peptides using an in vitro infant digestion model. After 28 days of storage, aged-only (AO) and frozen-then-aged (FA) beef exhibited higher α-amino group contents in the 10% trichloroacetic acid-soluble fraction compared to day 0 (P < 0.05). Following in vitro digestion in the infant model, FA showed higher contents of α-amino groups and smaller proteins (<3 and 1 kDa) than day 0 and AO (P < 0.05). Relative contributions of myofibrillar, sarcoplasmic, and stromal proteins to the bioactive peptides released from AO and FA differed from those of day 0. In addition, FA exhibited a higher proportion of potential bioactive peptide sequences. Overall, freezing-then-aging treatment can enhance the potential health benefits of beef to be used as a protein source for complementary foods.
Subject(s)
Peptides , Proteins , Infant , Animals , Cattle , Humans , Freezing , Peptides/chemistry , Gastrointestinal Tract , DigestionABSTRACT
This study investigated the effects of heating temperature of egg white gels (EWGs) on the digestive characteristics by heating egg white (EW) to reach 75 °C (EWG-75) and 95 °C (EWG-95). The gel protein structure showed a decrease in the maximum tryptophan fluorescence intensity and a significant increase in the surface hydrophobicity of EWGs compared to EW (P < 0.05). The total and reactive free sulfhydryl groups were higher in the EWGs than in the EW (P < 0.05). While the proportions of α-helical and ß-sheet structures remained similar in EW and EWG-75 (P > 0.05), EWG-95 exhibited a notable decrease in α-helix content (P < 0.05) and an increase in ß-sheet content (P < 0.05). Furthermore, EWG-95 displayed higher hardness and cohesiveness than EWG-75 (P < 0.05). In the adult and elderly in vitro digestion models, EWG-95 exhibited the highest protein digestibility (50.44 % and 54.65 % in the models of elderly and adult subjects, respectively) after GI digestion (P < 0.05), followed by EWG-75 and EW. The electrophoretogram of the digesta revealed more intense protein bands in the elderly digestion model, particularly in the gastric digesta of EW, indicating slower digestion compared to the adult model. Therefore, EW should be appropriately heated before consumption, especially for elderly individuals, to facilitate efficient protein digestion and absorption.
Subject(s)
Heating , Hot Temperature , Humans , Aged , Temperature , Egg Proteins/chemistry , DigestionABSTRACT
Pleomorphic adenoma (PA) is a benign tumor characterized by slow-growing mixed tumors in the craniofacial area. It is relatively common in salivary glands; however, PA of the nasal cavity, which arises in the minor salivary glands, is rare. We present the case of a large PA in the nasal cavity of an adult immunocompetent woman with nasal obstruction and intermittent epistaxis. Based on preoperative radiologic examinations, she was misdiagnosed with an inverted papilloma. Endoscopic resection was performed under general anesthesia. Pathologically, the patient was confirmed to have PA, which has great cellularity and few stromal components. No complications or recurrences during the 1-year follow-up period were observed.
Subject(s)
Adenoma, Pleomorphic , Nose Neoplasms , Papilloma, Inverted , Adult , Female , Humans , Nasal Cavity/surgery , Nasal Cavity/pathology , Adenoma, Pleomorphic/diagnosis , Adenoma, Pleomorphic/surgery , Adenoma, Pleomorphic/pathology , Papilloma, Inverted/diagnosis , Papilloma, Inverted/surgery , Nose Neoplasms/diagnosis , Nose Neoplasms/surgery , Nose Neoplasms/pathology , Diagnostic ErrorsABSTRACT
BACKGROUND/AIM: Currently, olaparib, a poly(ADP-ribose) polymerase (PARP) inhibitor, has been approved as maintenance therapy for patients with germline BRCA mutations and metastatic pancreatic cancer. However, platinum-based chemotherapy, which induces synthetic lethality with PARP inhibitor treatment, is still controversial. Hence, we aimed to examine a platinum-based drug in combination with a PARP inhibitor and generate data regarding the use of a PARP inhibitor in the overall treatment of pancreatic cancer. MATERIALS AND METHODS: Using the Capan-1 cell line (BRCA2-mutant pancreatic cancer cell line), we evaluated the combinatorial effects of olaparib, a PARP inhibitor, and oxaliplatin by cell viability, combination index, western blotting, immunocytochemistry, flow cytometry, apoptosis assays and in vivo experiments. RESULTS: Capan-1 cells showed high sensitivity to olaparib due to the alteration in PARP activity, which led to cell death through the accumulation of oxaliplatin-induced DNA damage. Beyond DNA damage, oxaliplatin also suppressed the CDK1/BRCA1 signaling axis, which induced defects in homologous recombination repair. Additionally, inhibition of CDK1, a biomarker for oxaliplatin efficacy, induced cell death regardless of the BRCA mutation profile. CONCLUSION: Oxaliplatin may be used in combination with olaparib in PDAC patients with DNA damage repair mutations. Our findings highlight CDK1 as a potential therapeutic target for pancreatic cancer.
Subject(s)
Pancreatic Neoplasms , Poly(ADP-ribose) Polymerase Inhibitors , Humans , Poly(ADP-ribose) Polymerase Inhibitors/pharmacology , Poly(ADP-ribose) Polymerase Inhibitors/therapeutic use , Oxaliplatin/pharmacology , DNA Repair , DNA Damage , Poly(ADP-ribose) Polymerases/metabolism , Pancreatic Neoplasms/drug therapy , Pancreatic Neoplasms/genetics , Phthalazines/pharmacology , Phthalazines/therapeutic use , BRCA1 Protein/genetics , BRCA1 Protein/metabolism , CDC2 Protein Kinase/metabolismABSTRACT
The solubility and structure of myosin and the properties of pork gel with NaCl, KCl, CaCl2, and MgCl2 were investigated. Myofibrillar proteins (MPs) with phosphate were more solubilized with NaCl than with KCl (p < 0.05). CaCl2 and MgCl2 showed lower MP solubilities than those of NaCl and KCl (p < 0.05). The α-helix content of myosin was lower in KCl, CaCl2, and MgCl2 than in NaCl (p < 0.05). The pH of pork batter decreased in the order of KCl, NaCl, MgCl2, and CaCl2 (p < 0.05). The cooking yield of the pork gel manufactured with monovalent salts was higher than that of the pork gel manufactured with divalent salts (p < 0.05). The pork gel manufactured with KCl and MgCl2 showed lower hardness than that of the pork gel manufactured with NaCl. The solubility and structure of myosin were different with the different chloride salts and those led the different quality properties of pork gel. Therefore, the results of this study can be helpful for understanding the quality properties of low-slat meat products manufactured by replacing sodium chloride with different chloride salts.
ABSTRACT
Processed meat products play a vital role in our daily dietary intake due to their rich protein content and the inherent convenience they offer. However, they often contain synthetic additives and ingredients that may pose health risks when taken excessively. This review explores strategies to improve meat product quality, focusing on three key approaches: substituting synthetic additives, reducing the ingredients potentially harmful when overconsumed like salt and animal fat, and boosting nutritional value. To replace synthetic additives, natural sources like celery and beet powders, as well as atmospheric cold plasma treatment, have been considered. However, for phosphates, the use of organic alternatives is limited due to the low phosphate content in natural substances. Thus, dietary fiber has been used to replicate phosphate functions by enhancing water retention and emulsion stability in meat products. Reducing the excessive salt and animal fat has garnered attention. Plant polysaccharides interact with water, fat, and proteins, improving gel formation and water retention, and enabling the development of low-salt and low-fat products. Replacing saturated fats with vegetable oils is also an option, but it requires techniques like Pickering emulsion or encapsulation to maintain product quality. These strategies aim to reduce or replace synthetic additives and ingredients that can potentially harm health. Dietary fiber offers numerous health benefits, including gut health improvement, calorie reduction, and blood glucose and lipid level regulation. Natural plant extracts not only enhance oxidative stability but also reduce potential carcinogens as antioxidants. Controlling protein and lipid bioavailability is also considered, especially for specific consumer groups like infants, the elderly, and individuals engaged in physical training with dietary management. Future research should explore the full potential of dietary fiber, encompassing synthetic additive substitution, salt and animal fat reduction, and nutritional enhancement. Additionally, optimal sources and dosages of polysaccharides should be determined, considering their distinct properties in interactions with water, proteins, and fats. This holistic approach holds promise for improving meat product quality with minimal processing.
ABSTRACT
In this study, concentration levels of beet powder (BP) and caramel color (CC) were optimized to simulate beef color in meat analogs before and after cooking. The central composite design of response surface methodology (RSM) was used to set the levels of BP and CC, and the CIE L*, CIE a*, and CIE b* were selected as the responses for RSM. After optimization, myoglobin-free beef patties were prepared with three optimized levels of BP and CC. When raw, all the patties had the same color as natural beef; however, CIE L*, CIE a*, and CIE b* were statistically different from those of beef after cooking (p<0.05). Moreover, the use of BP and CC induced "browning" after the cooking process, with no excessive yellow color. Therefore, based on the overall desirability in the color optimization using RSM, the combination of BP (1.32%) and CC (1.08%) with the highest overall desirability can be used to simulate the color change of beef in meat analogs.
ABSTRACT
Beef is an ideal protein source for use as a complementary food in infants. Considering the limited protein-digesting capacity of infants, it is required to enhance protein digestibility while minimizing the deterioration of beef quality. Thus, this study aimed to determine the effects of high-pressure processing (HPP) on the physicochemical properties and in vitro digestibility of beef proteins in an infant digestion model. HPP at 200 and 300 MPa decreased the tryptophan fluorescence intensity of the myosin and actin fractions relative to that at 0.1 MPa (P < 0.05). Compared to treatment at 0.1 and 100 MPa, HPP at 300 MPa decreased α-helix and ß-turn contents in the myosin and actin fractions (P < 0.05), whilst increasing the ß-sheet content (P < 0.05). Beef actomyosin content decreased (P < 0.05) during HPP at 200 and 300 MPa (c.f., 0.1 and 100 MPa). After in vitro digestion of beef, HPP at 200 and 300 MPa increased the α-amino group content and the abundance of proteins below 3 kDa in the digesta (P < 0.05). However, due to the considerable lipid oxidation at 300 MPa, HPP at 200 MPa is ideal for improving the protein digestibility of beef when incorporated into complementary foods for infants.
Subject(s)
Actins , Lipid Metabolism , Animals , Humans , Infant , Cattle , DigestionABSTRACT
The structural changes in emulsion products can be used to control the bioavailability of fatty acids and lipophilic compounds. After ingestion, lipid droplets undergo breakdown and structural changes as they pass through the gastrointestinal tract. The oil-water interface plays a critical role in modulating the digestive behavior of lipid droplets because changes in the interfacial layer control the adsorption of lipase and bile salts and determine the overall rate and extent of lipid digestion. Therefore, lipid digestibility can be tuned by selecting the appropriate types and levels of stabilizers. The stabilizer can change the lipase accessibility and exposure of lipid substrates, resulting in variable digestion rates. However, emulsified lipids are not only added to food matrixes but are also co-ingested from other dietary components. Therefore, overall consumption behaviors can affect the digestion rate and digestibility of emulsified lipids. Although designing an emulsion structure is challenging, controlling lipid digestion can improve the health benefits of products. Therefore, a thorough understanding of the process of emulsified lipid digestion is required to develop food products that enable specific physiological responses. The targeted or delayed release of lipophilic molecules and fatty acids through emulsion systems has significant applications in healthcare and pharmaceuticals.
ABSTRACT
The protein digestibility of beef at three prefreezing temperatures (freezing at -20 °C, F20; freezing at -50 °C, F50; and freezing at -70 °C, F70) and aging periods (4, 14, and 28 days) was investigated using an in vitro infant digestion model. The increased cathepsin B activity in the frozen-then-aged treatments (P < 0.05) resulted in a higher content of 10% trichloroacetic acid-soluble α-amino groups than in the aged-only group on days 14 and 28 (P < 0.05). F50 had the most α-amino groups in the digesta and digested proteins under 3 kDa on day 28 (P < 0.05), with the disappearance of actin band in the digesta electrophoretogram. The secondary and tertiary structures of myofibrillar proteins revealed that F50 underwent irreversible denaturation (P < 0.05), especially in the myosin fraction, while F20 and F70 showed protein renaturation during aging (P < 0.05). In general, prefreezing at -50 °C then aging can improve the in vitro protein digestibility of beef through freezing-induced structural changes.
ABSTRACT
To the best of our knowledge, few studies have utilized cold plasma to improve soybean protein extraction yield and the functional properties of soybean protein. In this study, we aimed to assess the benefits of remote plasma treatments on soybean with respect to the utilization of soybean protein. This study involved two different sample forms (whole and crushed beans), two different plasma chemistry modes (ozone and nitrogen oxides [NOx = NO + NO2]), and a novel pressure-swing reactor. Crushed soybeans were significantly affected by NOx-mode plasma treatment. Crushed soybeans treated with NOx-mode plasma had the best outcomes, wherein the protein extraction yield increased from 31.64% in the control to 37.90% after plasma treatment. The water binding capacity (205.50%) and oil absorption capacity (267.67%) of plasma-treated soybeans increased to 190.88% and 246.23 % of the control, respectively. The emulsifying activity and emulsion stability slightly increased compared to those of the control. The secondary structure and surface hydrophobicity were altered. The remote plasma treatment of crushed soybeans increased soybean protein extraction yield compared to plasma-treated whole beans as well as untreated beans and altered the structural and physicochemical properties of soybean proteins.
Subject(s)
Glycine max , Soybean Proteins , Soybean Proteins/chemistry , Glycine max/chemistry , Water , Chemical Phenomena , Hydrophobic and Hydrophilic InteractionsABSTRACT
This study investigated the protein digestibility of chicken breast and thigh in an in vitro digestion model to determine the better protein sources for the elderly in terms of bioavailability. For this purpose, the biochemical traits of raw muscles and the structural properties of myofibrillar proteins were monitored. The thigh had higher pH, 10% trichloroacetic acid-soluble α-amino groups, and protein carbonyl content than the breast (p<0.05). In the proximate composition, the thigh had higher crude fat and lower crude protein content than the breast (p<0.05). Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of myofibrillar proteins showed noticeable differences in the band intensities of tropomyosin α-chain and myosin light chain-3 between the thigh and breast. The intrinsic tryptophan fluorescence intensity of myosin was lower in the thigh than in the breast (p<0.05). Moreover, circular dichroism spectroscopy of myosin revealed that the thigh had higher α-helical and lower ß-sheet structures than the breast (p<0.05). The cooked muscles were then chopped and digested in the elderly digestion model. The thigh had more α-amino groups than the breast after both gastric and gastrointestinal digestion (p<0.05). SDS-PAGE analysis of the gastric digesta showed that more bands remained in the digesta of the breast than that of the thigh. The content of proteins less than 3 kDa in the gastrointestinal digesta was also higher in the thigh than in the breast (p<0.05). These results reveal that chicken thigh with higher in vitro protein digestibility is a more appropriate protein source for the elderly than chicken breast.
ABSTRACT
This study investigated the predictability of cooking loss of pork loin through relatively easy and quick measurable quality properties. The pH, color, moisture, protein content, and cooking loss of 100 pork loins were measured. The explanatory variables included in all linear regression models with an adjust-r2 value of ≥0.5 were pH and the protein content. In the linear regression model predicting cooking loss, the highest adjust-r2 value was 0.7, with pH, CIE L*, CIE b*, moisture, and protein content as the explanatory variables. In 30 pork loins, electrical conductivity was additionally measured, and as a result of linear regression analysis for predicting cooking loss, the highest adjust-r2 value was 0.646 with electrical conductivity measured at 40 Hz, with pH and color as the explanatory variables. Ordinal logistic regression analysis was performed to predict the three grades (low, middle, and high) of loin cooking loss using pH, color, and 40 Hz electrical conductivity as the explanatory variables, and the percent concordance was 93.8%. In conclusion, the addition of electrical conductivity as an explanatory variable did not increase the prediction accuracy of the linear regression model for predicting cooking loss; however, it was demonstrated that it is possible to predict and classify the cooking loss grade of pork loin through quality properties that can be measured quickly and easily.
ABSTRACT
BACKGROUND/AIM: This study evaluated the clinical implications of epithelial-mesenchymal transition (EMT) markers and peritumoral immune cell infiltration in patients with biliary tract cancer (BTC) treated with gemcitabine plus cisplatin (GemCis). MATERIALS AND METHODS: Forty-five patients with advanced BTC who received GemCis were included as the study population. We conducted multiplex immunohistochemistry and examined EMT markers and their correlations with immune cell infiltrate at the invasive tumor margin. Study population was subdivided into two groups: twenty-four patients with overall survival (OS) less than 10 months (short-term survivor group, SS) and 21 with OS of 20 months or longer (long-term survivor group, LS). RESULTS: The density of tumor cells expressing epithelial marker E-cadherin (E-cadherin+ CK+) at the invasive tumor margin tended to be higher in the LS group than that in the SS group (p=0.065). The density of tumor cells expressing mesenchymal marker vimentin (vimentin+ CK+) was significantly higher in the SS group than that in the LS group (p=0.021). The density of E-cadherin- vimentin+ tumor cells (E-cadherin- vimentin+ CK+) was also significantly higher in the SS group (p=0.020). The density of OX40 expressing cells was significantly higher in the SS group compared to that in the LS group (p=0.006). The density of vimentin-expressing tumor cells was positively correlated with FoxP3+ CD4+ regulatory T-cells (r=0.29, p=0.047) and OX40+ cells (r=0.48, p<0.001). CONCLUSION: EMT-related features were enriched in BTC patients with poor survival outcomes and associated with regulatory T-cell infiltration.
Subject(s)
Bile Duct Neoplasms , Biliary Tract Neoplasms , Humans , Epithelial-Mesenchymal Transition/genetics , Vimentin/genetics , Cadherins/genetics , Bile Duct Neoplasms/drug therapy , Biliary Tract Neoplasms/pathology , Deoxycytidine/therapeutic use , Phenotype , Biomarkers, TumorABSTRACT
This study investigated the physicochemical characteristics of pork emulsion gels manufactured from hot-boned (HB) pork and winter mushroom powder in the absence of phosphate. It was found that compared to cold-boned (CB) pork, HB pork had a higher pH and exhibited a higher myofibrillar protein solubility with a lower actomyosin content (P < 0.05). Four types of pork gels were prepared, namely CB pork without phosphate, CB pork with phosphate (CBP), HB pork without phosphate, and HB pork with winter mushroom powder but without phosphate (HBW). The total exuded fluid was comparable for the CBP and HBW gels on all storage days. In addition, the HB and HBW gels had similar springiness and cohesiveness properties to the CBP gel (P > 0.05). These results indicate that the quality of pork gels manufactured in the absence of phosphate can be improved by the use of HB pork and with the incorporation of winter mushroom powder.