Pub Date : 2026-02-01DOI: 10.1016/j.fochx.2026.103555
Tiantian Wang , Haijing Wu , Qianyu Hang , Siqi Zhao , Leiqing Pan , Chao Ding , Qiang Liu
Lipid hydrolysis catalyzed by endogenous lipases is a major contributor to quality deterioration in stored rice. This study aimed to elucidate how cold plasma (CP) treatment affects lipid stability by examining changes in lipase activity, structure, and endogenous ferulic acid (FA) during storage. After 60 days, CP-treated rice showed a 15.8% increase in FA content, accompanied by a 22.4% reduction in lipase activity and an approximately 25% decrease in free fatty acid value compared with the control. FT-IR spectroscopy revealed alterations in lipase secondary structure, including decreased α-helix (2.1%) and β-sheet (5.7%) and an increased random coil content (12.7%). Molecular docking confirmed FA binding within the active site via hydrophobic/hydrogen bonds, sterically hindering substrate access. Enzyme kinetic analysis showed that FA decreased Vmax while increasing Km, indicating mixed-type inhibition. Overall, CP treatment is associated with coordinated regulation of lipase structure and activity, contributing to improved lipid stability during storage.
{"title":"Revealing the inhibitory mechanism of ferulic acid on rice lipase via structural and kinetic analyses under cold plasma treatment during storage","authors":"Tiantian Wang , Haijing Wu , Qianyu Hang , Siqi Zhao , Leiqing Pan , Chao Ding , Qiang Liu","doi":"10.1016/j.fochx.2026.103555","DOIUrl":"10.1016/j.fochx.2026.103555","url":null,"abstract":"<div><div>Lipid hydrolysis catalyzed by endogenous lipases is a major contributor to quality deterioration in stored rice. This study aimed to elucidate how cold plasma (CP) treatment affects lipid stability by examining changes in lipase activity, structure, and endogenous ferulic acid (FA) during storage. After 60 days, CP-treated rice showed a 15.8% increase in FA content, accompanied by a 22.4% reduction in lipase activity and an approximately 25% decrease in free fatty acid value compared with the control. FT-IR spectroscopy revealed alterations in lipase secondary structure, including decreased α-helix (2.1%) and β-sheet (5.7%) and an increased random coil content (12.7%). Molecular docking confirmed FA binding within the active site via hydrophobic/hydrogen bonds, sterically hindering substrate access. Enzyme kinetic analysis showed that FA decreased V<sub>max</sub> while increasing K<sub>m</sub>, indicating mixed-type inhibition. Overall, CP treatment is associated with coordinated regulation of lipase structure and activity, contributing to improved lipid stability during storage.</div></div>","PeriodicalId":12334,"journal":{"name":"Food Chemistry: X","volume":"34 ","pages":"Article 103555"},"PeriodicalIF":8.2,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146075636","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
This study systematically explored the impact of steaming processing on Citri Sarcodactylis Fructus, focusing on changes in aroma, "dryness-like" properties, and the underlying chemical mechanisms. By employing HS-GC-MS, UHPLC-MS, electronic nose analysis, and animal experiments, we found that steaming triggered distinct changes in flavor substances: fresh, citrus-like volatiles diminished, while woody and bitter compounds increased, leading to a more intense aroma. It also drove the transformation of active components: flavonoid glycosides were converted to aglycones, with coumarins and limonoids were rearranged. These changes alleviated "dryness-like" effects: steamed CSF reduced rat water intake and blood viscosity (p < 0.05), normalized the aquaporins expression. Molecular and cellular assays linked this to stronger aglycone-AQP binding and weaker glycoside-induced AQP5 inhibition, which directly linked steaming to reduced dryness. This research clarified how steaming enhances aroma complexity and reduces "dryness-like" properties through targeted chemical transformations, providing a scientific basis for optimizing CSF processing via steaming.
{"title":"Effects of steam processing conditions on the aroma and \"dryness-like\" effect of <i>Citri Sarcodactylis fructus</i>(FoShou tea).","authors":"Xinhang Cai, Lishan Chen, Wangjun Li, Hu Wang, Yue Sun, Xingyang Xue, Shumei Wang, Menghua Wu, Jiang Meng","doi":"10.1016/j.fochx.2026.103590","DOIUrl":"10.1016/j.fochx.2026.103590","url":null,"abstract":"<p><p>This study systematically explored the impact of steaming processing on <i>Citri Sarcodactylis Fructus</i>, focusing on changes in aroma, \"dryness-like\" properties, and the underlying chemical mechanisms. By employing HS-GC-MS, UHPLC-MS, electronic nose analysis, and animal experiments, we found that steaming triggered distinct changes in flavor substances: fresh, citrus-like volatiles diminished, while woody and bitter compounds increased, leading to a more intense aroma. It also drove the transformation of active components: flavonoid glycosides were converted to aglycones, with coumarins and limonoids were rearranged. These changes alleviated \"dryness-like\" effects: steamed CSF reduced rat water intake and blood viscosity (<i>p</i> < 0.05), normalized the aquaporins expression. Molecular and cellular assays linked this to stronger aglycone-AQP binding and weaker glycoside-induced AQP5 inhibition, which directly linked steaming to reduced dryness. This research clarified how steaming enhances aroma complexity and reduces \"dryness-like\" properties through targeted chemical transformations, providing a scientific basis for optimizing CSF processing via steaming.</p>","PeriodicalId":12334,"journal":{"name":"Food Chemistry: X","volume":"34 ","pages":"103590"},"PeriodicalIF":8.2,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12887779/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146164766","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-02-01DOI: 10.1016/j.fochx.2026.103565
Jianwei Fan, Haoyuan Wang, Zhilong Zeng, Yijia Li, Xiaoli Qin, Yao Li, Xiong Liu
The cryoprotective effects of deacetylated konjac glucomannan (DKGM) on gluten and its components in frozen dough remain unclear. This study aimed to investigate the impact of DKGM with varying degrees of deacetylation (DD) on the structural stability of gluten and its components during freeze-thaw (FT) cycles. Compared with konjac glucomannan, DKGM effectively alleviated the gluten structural "depolymerization-aggregation" process during FT cycles, with DK2 (DD, 50.21%) exhibiting the optimal cryoprotective effect. The DK2 group retained higher noncovalent interactions and disulfide bonds during FT cycles, thereby stabilizing the gluten structure. Studies on glutenin and gliadin suggest that glutenin is more susceptible to FT damage. DK2 provided the best protection for glutenin, whereas DK3 (DD, 66.61%) provided the most effective protection for gliadin. These distinct effects were likely attributable to differences in the particle size and steric hindrance of DKGM, as well as the inherent structural characteristics of the protein components.
{"title":"Alleviation of structural deterioration in gluten and its components during freeze-thaw cycles by deacetylated konjac glucomannan.","authors":"Jianwei Fan, Haoyuan Wang, Zhilong Zeng, Yijia Li, Xiaoli Qin, Yao Li, Xiong Liu","doi":"10.1016/j.fochx.2026.103565","DOIUrl":"10.1016/j.fochx.2026.103565","url":null,"abstract":"<p><p>The cryoprotective effects of deacetylated konjac glucomannan (DKGM) on gluten and its components in frozen dough remain unclear. This study aimed to investigate the impact of DKGM with varying degrees of deacetylation (DD) on the structural stability of gluten and its components during freeze-thaw (FT) cycles. Compared with konjac glucomannan, DKGM effectively alleviated the gluten structural \"depolymerization-aggregation\" process during FT cycles, with DK2 (DD, 50.21%) exhibiting the optimal cryoprotective effect. The DK2 group retained higher noncovalent interactions and disulfide bonds during FT cycles, thereby stabilizing the gluten structure. Studies on glutenin and gliadin suggest that glutenin is more susceptible to FT damage. DK2 provided the best protection for glutenin, whereas DK3 (DD, 66.61%) provided the most effective protection for gliadin. These distinct effects were likely attributable to differences in the particle size and steric hindrance of DKGM, as well as the inherent structural characteristics of the protein components.</p>","PeriodicalId":12334,"journal":{"name":"Food Chemistry: X","volume":"34 ","pages":"103565"},"PeriodicalIF":8.2,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12906197/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146200602","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-02-01DOI: 10.1016/j.fochx.2026.103627
Haijun Chang, Xin Wen, Yu Huang, Yu Hu, Yuanwei Shi
The research aimed to elucidate the interaction and mechanism between the Portulaca oleracea L. extract (POE) and the pork myofibrillar proteins (MPs) from the perspectives of fluorescence spectroscopy and molecular docking. The results showed that POE significantly increased intermolecular hydrogen bonds and hydrophobic interactions in MPs (P < 0.05). Among the non-covalent forces between POE and MPs, hydrophobic interactions were dominant followed by hydrogen bonds. POE would cause a decrease in the endogenous fluorescence intensity of MPs, and the quenching type was static quenching. The binding molar ratio of POE to MPs was 1:1, and the formed complex exhibited high stability. The thermodynamic constants ∆G < 0, ∆H > 0, and ∆S > 0 indicated that the binding process between POE and MPs was spontaneous, with hydrophobic interactions being the primary driving force. Additionally, the nine most abundant compounds in POE were selected for molecular docking with myosin, and the binding energies were all negative, confirming that POE could spontaneously interact with MPs. The molecular docking results further demonstrated that hydrophobic interactions and hydrogen bonding were the main binding forces, with Leu270 potentially serving as a key amino acid residue in the interaction between POE and MPs. This study provides valuable insights into the molecular interactions between Portulaca oleracea L. extract and pork myofibrillar proteins, offering a theoretical basis for phenolic small molecule substances in regulating protein oxidation and potential applications in improving meat product quality.
本研究旨在从荧光光谱和分子对接的角度探讨马蹄苋提取物（porulaca oleracea L. extract， POE）与猪肉肌原纤维蛋白（myofibrar proteins, MPs）的相互作用及其机制。结果表明，POE显著增加了MPs分子间氢键和疏水相互作用（P 0），∆S >表明POE与MPs的结合过程是自发的，疏水相互作用是主要驱动力。此外，我们选择POE中最丰富的9个化合物与myosin进行分子对接，结合能均为负，证实POE可以自发地与MPs相互作用。分子对接结果进一步表明，疏水相互作用和氢键是主要的结合力，而Leu270可能是POE与MPs相互作用的关键氨基酸残基。本研究为马齿苋提取物与猪肉肌原纤维蛋白的分子相互作用提供了有价值的见解，为酚类小分子物质调节蛋白质氧化和改善肉制品品质提供了理论依据。
{"title":"Mechanism of interaction between <i>Portulaca oleracea</i> L. extract and pork myofibrillar protein: Insights from spectroscopic and molecular docking analyses.","authors":"Haijun Chang, Xin Wen, Yu Huang, Yu Hu, Yuanwei Shi","doi":"10.1016/j.fochx.2026.103627","DOIUrl":"10.1016/j.fochx.2026.103627","url":null,"abstract":"<p><p>The research aimed to elucidate the interaction and mechanism between the <i>Portulaca oleracea</i> L. extract (POE) and the pork myofibrillar proteins (MPs) from the perspectives of fluorescence spectroscopy and molecular docking. The results showed that POE significantly increased intermolecular hydrogen bonds and hydrophobic interactions in MPs (<i>P</i> < 0.05). Among the non-covalent forces between POE and MPs, hydrophobic interactions were dominant followed by hydrogen bonds. POE would cause a decrease in the endogenous fluorescence intensity of MPs, and the quenching type was static quenching. The binding molar ratio of POE to MPs was 1:1, and the formed complex exhibited high stability. The thermodynamic constants ∆G < 0, ∆H > 0, and ∆S > 0 indicated that the binding process between POE and MPs was spontaneous, with hydrophobic interactions being the primary driving force. Additionally, the nine most abundant compounds in POE were selected for molecular docking with myosin, and the binding energies were all negative, confirming that POE could spontaneously interact with MPs. The molecular docking results further demonstrated that hydrophobic interactions and hydrogen bonding were the main binding forces, with Leu270 potentially serving as a key amino acid residue in the interaction between POE and MPs. This study provides valuable insights into the molecular interactions between <i>Portulaca oleracea</i> L. extract and pork myofibrillar proteins, offering a theoretical basis for phenolic small molecule substances in regulating protein oxidation and potential applications in improving meat product quality.</p>","PeriodicalId":12334,"journal":{"name":"Food Chemistry: X","volume":"34 ","pages":"103627"},"PeriodicalIF":8.2,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12887781/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146164800","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-02-01DOI: 10.1016/j.fochx.2026.103586
Yajin Zhang , Huiyuan Jin , Hongwei Song , Ramy M. Khoder , Shanbai Xiong , Tao Yin , Ru Liu , Qilin Huang , Juan You
To preserve the structure and quality of critical edible regions in frozen bighead carp (BHC) heads. Air freezing (AF, −30 °C), composite immersion freezing (CIF, −30 °C), and liquid nitrogen spray freezing (LNSF, −90 °C) were compared for the effects on the water status, ice morphology, microstructure, protein characteristics, and lipid oxidation of gill side flesh (GSF) and collar flesh (CF). Dendritic ice crystals formed in AF samples, fracturing collagen fibers. CIF and LNSF promoted spherical ice, preserving adipocytes and collagen structure. LNSF reduced water migration, maintained the α-helix content (27.68%), and suppressed protein unfolding in GSF, resulting in smoother and intact surfaces of the muscle bundles. LNSF treated CF showed the lowest values of malondialdehyde (0.27 mg/kg), acid value (1.53 mg/g), and peroxide value (5.01 mmol/kg). Overall, the quality of BHC heads was preserved by LNSF at −90 °C. This study establishes freezing technological for frozen fish heads.
{"title":"Differential freezing responses in gill side flesh vs. collar flesh of bighead carp (Aristichthys nobilis) head: the role of ice crystal formation in protein and lipid deterioration","authors":"Yajin Zhang , Huiyuan Jin , Hongwei Song , Ramy M. Khoder , Shanbai Xiong , Tao Yin , Ru Liu , Qilin Huang , Juan You","doi":"10.1016/j.fochx.2026.103586","DOIUrl":"10.1016/j.fochx.2026.103586","url":null,"abstract":"<div><div>To preserve the structure and quality of critical edible regions in frozen bighead carp (BHC) heads. Air freezing (AF, −30 °C), composite immersion freezing (CIF, −30 °C), and liquid nitrogen spray freezing (LNSF, −90 °C) were compared for the effects on the water status, ice morphology, microstructure, protein characteristics, and lipid oxidation of gill side flesh (GSF) and collar flesh (CF). Dendritic ice crystals formed in AF samples, fracturing collagen fibers. CIF and LNSF promoted spherical ice, preserving adipocytes and collagen structure. LNSF reduced water migration, maintained the α-helix content (27.68%), and suppressed protein unfolding in GSF, resulting in smoother and intact surfaces of the muscle bundles. LNSF treated CF showed the lowest values of malondialdehyde (0.27 mg/kg), acid value (1.53 mg/g), and peroxide value (5.01 mmol/kg). Overall, the quality of BHC heads was preserved by LNSF at −90 °C. This study establishes freezing technological for frozen fish heads.</div></div>","PeriodicalId":12334,"journal":{"name":"Food Chemistry: X","volume":"34 ","pages":"Article 103586"},"PeriodicalIF":8.2,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146075555","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Anthocyanins are water-soluble flavonoid pigments responsible for red, purple, and blue hues in plant tissues. Rosaceae fruits—including blackberries, raspberries, strawberries, cherries, and apples—are rich sources of anthocyanins with notable antioxidant potential. This review highlights the diversity, extraction techniques, bioactivity, and applications of anthocyanins from Rosaceae fruits. A total of 37 compounds were identified, dominated by cyanidin, delphinidin, and pelargonidin derivatives, reflecting active biosynthetic pathways via F3′H and F3′5′H enzymes. Structural variation is influenced by glycosylation and acylation, involving glucoside, galactoside, rutinoside, and malonyl-glucoside forms. In vitro and in vivo studies demonstrate antioxidant, anti-inflammatory, antidiabetic, anti-obesity, anticancer, and antibacterial effects. Anthocyanin-rich extracts show promise as natural food colorants, offering safer alternatives to synthetic dyes. Encapsulation and copigmentation strategies further enhance their stability and functionality. These findings support the potential of Rosaceae-derived anthocyanins in health-promoting formulations and sustainable food applications
{"title":"Anthocyanins from Rosaceae fruits: diversity, bioactivity, and potential as natural colorants","authors":"Muhammad Habibul Ikhsan , Selvi Apriliana Putri , Herlandita Rona Anggraeni , Rika Septiyanti , Ari Hardianto , Jalifah Latip , Tati Herlina","doi":"10.1016/j.fochx.2026.103606","DOIUrl":"10.1016/j.fochx.2026.103606","url":null,"abstract":"<div><div>Anthocyanins are water-soluble flavonoid pigments responsible for red, purple, and blue hues in plant tissues. Rosaceae fruits—including blackberries, raspberries, strawberries, cherries, and apples—are rich sources of anthocyanins with notable antioxidant potential. This review highlights the diversity, extraction techniques, bioactivity, and applications of anthocyanins from Rosaceae fruits. A total of 37 compounds were identified, dominated by cyanidin, delphinidin, and pelargonidin derivatives, reflecting active biosynthetic pathways via F3′H and F3′5′H enzymes. Structural variation is influenced by glycosylation and acylation, involving glucoside, galactoside, rutinoside, and malonyl-glucoside forms. In vitro and in vivo studies demonstrate antioxidant, anti-inflammatory, antidiabetic, anti-obesity, anticancer, and antibacterial effects. Anthocyanin-rich extracts show promise as natural food colorants, offering safer alternatives to synthetic dyes. Encapsulation and copigmentation strategies further enhance their stability and functionality. These findings support the potential of Rosaceae-derived anthocyanins in health-promoting formulations and sustainable food applications</div></div>","PeriodicalId":12334,"journal":{"name":"Food Chemistry: X","volume":"34 ","pages":"Article 103606"},"PeriodicalIF":8.2,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146075660","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Probiotics suffer low viability from heat and oxidative stress during spray drying. This study evaluated alkaline-pH-shifted mung bean protein isolate (pHMBPI) as an encapsulant for Limosilactobacillus reuteri KUB-AC5, compared with mung bean protein isolate (MBPI) and whey protein isolate (WPI). pHMBPI showed the highest solubility (82.66%), surface hydrophobicity (3574), and ABTS•+ scavenging activity (91.62%). pHMBPI-spray-dried cells had the lowest cell wall (25.31%) and membrane injury (10.22%), the highest viable count (1.49 × 109 CFU/g) and survival (9.91%). Viability during digestion remained high (8.60 and 8.05 log CFU/g in gastric and intestinal fluids). NMR confirmed reduced lipid peroxidation, preserving 85.2% of bis-allylic protons. Molecular dynamics simulations revealed strong electrostatic interactions between 8S-alpha globulin and cell wall targets, including peptidoglycan, Mub-RV, and SRRP53608. These results identify pHMBPI as a promising encapsulant offering enhanced thermal stability, antioxidant defense, and targeted bacterial surface binding.
{"title":"Alkaline-pH-shifted mung bean protein isolate for spray-dried probiotic encapsulation: Insights into molecular cell wall interactions and oxidative protection","authors":"Akkaratch Rodklongtan , Patharapim Laurujisawat , Thatchawan Dumrongchai , Wansiri Innok , Borvornwat Toviwek , Prapasiri Pongprayoon , Pakamon Chitprasert","doi":"10.1016/j.fochx.2026.103562","DOIUrl":"10.1016/j.fochx.2026.103562","url":null,"abstract":"<div><div>Probiotics suffer low viability from heat and oxidative stress during spray drying. This study evaluated alkaline-pH-shifted mung bean protein isolate (pHMBPI) as an encapsulant for <em>Limosilactobacillus reuteri</em> KUB-AC5, compared with mung bean protein isolate (MBPI) and whey protein isolate (WPI). pHMBPI showed the highest solubility (82.66%), surface hydrophobicity (3574), and ABTS•<sup>+</sup> scavenging activity (91.62%). pHMBPI-spray-dried cells had the lowest cell wall (25.31%) and membrane injury (10.22%), the highest viable count (1.49 × 10<sup>9</sup> CFU/g) and survival (9.91%). Viability during digestion remained high (8.60 and 8.05 log CFU/g in gastric and intestinal fluids). NMR confirmed reduced lipid peroxidation, preserving 85.2% of bis-allylic protons. Molecular dynamics simulations revealed strong electrostatic interactions between 8S-alpha globulin and cell wall targets, including peptidoglycan, Mub-RV, and SRRP53608. These results identify pHMBPI as a promising encapsulant offering enhanced thermal stability, antioxidant defense, and targeted bacterial surface binding.</div></div>","PeriodicalId":12334,"journal":{"name":"Food Chemistry: X","volume":"34 ","pages":"Article 103562"},"PeriodicalIF":8.2,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146075612","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Sequential roasting is a unique technology for processing of Lu’an Guapian green tea. The chemical base and the mechanisms underpinning roasting-induced flavor and aroma changes are not fully understood. Here, variations in volatiles, catechins, and free amino acids were quantitatively measured, four epi-catechins and seven amino acids were significantly decreased, while gallocatechin and four phenylpropanoid volatiles (benzaldehyde, phenyl acetaldehyde, benzyl nitrile, and indole) were significantly increased. Modeling experiments suggest that benzyl alcohol, benzaldehyde, and phenyl acetaldehyde could be derived from phenylalanine pyrolysis and phenylalanine/glucose Maillard reaction, while indole could be derived from tryptophan pyrolysis and tryptophan/glucose Maillard reaction. In addition, phenyl acetaldehyde could be synthesized through tyrosine/glucose Maillard reaction. Gallocatechin, epigallocatechin, and gallocatechin gallate showed inhibition or activation toward aromatic amino acid pyrolysis or Maillard reaction in an amino acid- and gallocatechin isomer-specific manner. This study provided mechanistic insights about phenylpropanoid volatile synthesis and the roles of gallocatechin isomers during sequential roasting of Lu’an Guapian green tea.
{"title":"Phenylpropanoid volatile synthesis during sequential roasting of Lu’an Guapian green tea: Differential activities of gallocatechin isomers in aromatic amino acid pyrolysis and Maillard reactions","authors":"Mingjie Chen , Dongsheng Fang , Hongyu Yuan , Wei Zhang","doi":"10.1016/j.fochx.2026.103582","DOIUrl":"10.1016/j.fochx.2026.103582","url":null,"abstract":"<div><div>Sequential roasting is a unique technology for processing of Lu’an Guapian green tea. The chemical base and the mechanisms underpinning roasting-induced flavor and aroma changes are not fully understood. Here, variations in volatiles, catechins, and free amino acids were quantitatively measured, four epi-catechins and seven amino acids were significantly decreased, while gallocatechin and four phenylpropanoid volatiles (benzaldehyde, phenyl acetaldehyde, benzyl nitrile, and indole) were significantly increased. Modeling experiments suggest that benzyl alcohol, benzaldehyde, and phenyl acetaldehyde could be derived from phenylalanine pyrolysis and phenylalanine/glucose Maillard reaction, while indole could be derived from tryptophan pyrolysis and tryptophan/glucose Maillard reaction. In addition, phenyl acetaldehyde could be synthesized through tyrosine/glucose Maillard reaction. Gallocatechin, epigallocatechin, and gallocatechin gallate showed inhibition or activation toward aromatic amino acid pyrolysis or Maillard reaction in an amino acid- and gallocatechin isomer-specific manner. This study provided mechanistic insights about phenylpropanoid volatile synthesis and the roles of gallocatechin isomers during sequential roasting of Lu’an Guapian green tea.</div></div>","PeriodicalId":12334,"journal":{"name":"Food Chemistry: X","volume":"34 ","pages":"Article 103582"},"PeriodicalIF":8.2,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146075661","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-02-01DOI: 10.1016/j.fochx.2026.103602
Jiao Liu , Farah Zaaboul , Yanling Cheng , Ruizhi Yang , Luping Zhao
The present study was designed to determine the composition, emulsion properties and microencapsulation efficiency of Zanthoxylum oil bodies (ZOBs) at pH values of 6.3 and 11.0, employing soy protein isolate (SPI) and maltodextrin (MD) as wall materials. The findings indicated that pH 11.0-ZOBs exhibited improved emulsion stability and encapsulation efficiency was higher compared to pH 6.3-ZOBs. Across pH 11.0 and pH 6.3, the optimal SPI:MD ratios (1:3 and 1:4, respectively) resulted in increased encapsulation yields (86.83% and 81.58%, respectively) and the least surface oil. The combined effects of pH and wall material composition significantly affected emulsion stability, particle size and solubility (p < 0.05) with pH 11.0-ZOBs showing the greatest thermal and oxidative stability. Such correlations verify the significance of pH and wall material optimization for the isolation and microencapsulation OBs, providing insights to enhance the stability and functionality of encapsulated oils.
{"title":"Development and characterization of Zanthoxylum bungeanum seed kernel oil bodies with maltodextrin-soy protein isolate complex","authors":"Jiao Liu , Farah Zaaboul , Yanling Cheng , Ruizhi Yang , Luping Zhao","doi":"10.1016/j.fochx.2026.103602","DOIUrl":"10.1016/j.fochx.2026.103602","url":null,"abstract":"<div><div>The present study was designed to determine the composition, emulsion properties and microencapsulation efficiency of Zanthoxylum oil bodies (ZOBs) at pH values<!--> <!-->of 6.3 and 11.0, employing soy protein isolate (SPI) and maltodextrin (MD) as wall materials. The findings indicated that pH 11.0-ZOBs exhibited improved emulsion stability and encapsulation efficiency was higher compared to pH 6.3-ZOBs. Across pH 11.0 and pH 6.3, the optimal SPI:MD ratios (1:3 and<!--> <!-->1:4, respectively) resulted in increased encapsulation yields (86.83% and 81.58%, respectively) and the least surface oil. The combined effects of pH and wall material composition significantly affected emulsion stability, particle size<!--> <!-->and solubility (<em>p < 0.05</em>) with pH 11.0-ZOBs showing the greatest thermal and oxidative stability. Such correlations verify the significance of pH and wall material optimization for the isolation and microencapsulation OBs, providing insights to enhance the stability and functionality<!--> <!-->of encapsulated oils.</div></div>","PeriodicalId":12334,"journal":{"name":"Food Chemistry: X","volume":"34 ","pages":"Article 103602"},"PeriodicalIF":8.2,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146075611","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-02-01DOI: 10.1016/j.fochx.2026.103596
Youzhi Zhao , Fengxian Qin , Yanzhuo Liu , Naiqun Zhao , Mingjie Hu , Liankui Wen , Xinyao Liu , Zhitong Wang
This study investigated how high hydrostatic pressure (HHP) modulates the structural and functional properties of whey protein isolate (WPI) complexes with Malvidin-3-O-6-[acrylic acid-(2-hydroxy,4-carboxy-cyclohexanol) ester]-guaiacol (MV3ACEC). HHP at 350 MPa maximized the binding ratio (78.41 ± 0.94%) and thermal stability (denaturation temperature: 123.76 °C) of WPI-MV3ACEC, while reducing particle size (237 nm) and enhancing system stability (zeta potential: 12.7 mV). Structural analyses revealed HHP-induced conformational changes in WPI-MV3ACEC, including decreased α-helix and increased β-sheet content. Molecular simulations confirmed optimal binding affinity (−7.8 kcal/mol) at 350 MPa, dominated by van der Waals forces. HHP-treated complexes retained antioxidant activity and improved gastrointestinal stability, with MV3ACEC retention reaching 38.17% ± 0.86% post-intestinal digestion. These findings elucidate the binding mechanisms between WPI and MV3ACEC under HHP, providing novel insights for designing functional dairy products.
本文研究了高静水压力（HHP）如何调节乳清分离蛋白（WPI）与马来酸-3- o -6-[丙烯酸-（2-羟基，4-羧基环己醇）酯]-愈创木酚（MV3ACEC）配合物的结构和功能特性。350 MPa的高温高压使WPI-MV3ACEC的结合比（78.41±0.94%）和热稳定性（变性温度：123.76℃）达到最大，同时使WPI-MV3ACEC的粒径减小（237 nm），体系稳定性提高（zeta电位：12.7 mV）。结构分析显示hhp诱导的WPI-MV3ACEC构象发生变化，包括α-螺旋减少和β-薄片含量增加。分子模拟结果表明，在350 MPa下，范德华力主导的结合亲和力为- 7.8 kcal/mol。经hhp处理的复合物保留了抗氧化活性，改善了胃肠道稳定性，肠道消化后MV3ACEC保留率达到38.17%±0.86%。这些发现阐明了HHP下WPI与MV3ACEC的结合机制，为设计功能性乳制品提供了新的见解。
{"title":"High hydrostatic pressure modulation of whey protein-malvidin derivative complexes: Mechanisms, structural changes, and stability","authors":"Youzhi Zhao , Fengxian Qin , Yanzhuo Liu , Naiqun Zhao , Mingjie Hu , Liankui Wen , Xinyao Liu , Zhitong Wang","doi":"10.1016/j.fochx.2026.103596","DOIUrl":"10.1016/j.fochx.2026.103596","url":null,"abstract":"<div><div>This study investigated how high hydrostatic pressure (HHP) modulates the structural and functional properties of whey protein isolate (WPI) complexes with Malvidin-3-O-6-[acrylic acid-(2-hydroxy,4-carboxy-cyclohexanol) ester]-guaiacol (MV3ACEC). HHP at 350 MPa maximized the binding ratio (78.41 ± 0.94%) and thermal stability (denaturation temperature: 123.76 °C) of WPI-MV3ACEC, while reducing particle size (237 nm) and enhancing system stability (zeta potential: 12.7 mV). Structural analyses revealed HHP-induced conformational changes in WPI-MV3ACEC, including decreased α-helix and increased β-sheet content. Molecular simulations confirmed optimal binding affinity (−7.8 kcal/mol) at 350 MPa, dominated by van der Waals forces. HHP-treated complexes retained antioxidant activity and improved gastrointestinal stability, with MV3ACEC retention reaching 38.17% ± 0.86% post-intestinal digestion. These findings elucidate the binding mechanisms between WPI and MV3ACEC under HHP, providing novel insights for designing functional dairy products.</div></div>","PeriodicalId":12334,"journal":{"name":"Food Chemistry: X","volume":"34 ","pages":"Article 103596"},"PeriodicalIF":8.2,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146075619","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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