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Effects of refrigeration-induced protein oxidation of rice and wheat steamed bread on the human gut microbiota in an in vitro fermentation model
IF 6 1区 农林科学 Q1 FOOD SCIENCE & TECHNOLOGY Pub Date : 2025-03-16 DOI: 10.1016/j.lwt.2025.117657
Qiong Wu , Xiaojie Cui , Yuhui Yang , Keying Chu , Ru Liu , Sijin Gao , Yanli Xie
Rice and wheat steamed bread are common staple foods and important protein sources in the human diet. They are often prepared and refrigerated for later consumption. Here, we explored the influences of refrigeration on protein oxidation in rice and wheat steamed bread and investigated the effects of the resulting oxidized proteins on the human gut microbiota using an in vitro fermentation model. We found that as refrigeration time increased, the levels of protein oxidation products, including carbonyl groups and advanced glycation end products, in rice and wheat steamed bread increased, whereas those of free sulfhydryl and free amino groups decreased. The levels of specific amino acids (tyrosine, tryptophan, and glutamic acid) decreased with refrigeration, whereas those of amino acid oxidation products (dityrosine, N′-formylkynurenine, and kynurenine) increased. Furthermore, the relative abundance of potentially harmful bacteria, particularly Sutterella and Tyzzerella, increased, whereas that of probiotics, particularly Bifidobacterium and Phascolarctobacterium, decreased when rice and steamed bread proteins subjected to different refrigeration times were fermented with human gut microbiota. Moreover, the concentrations of short-chain fatty acids (acetate, propionate, and butyrate) in fermentation broth decreased with refrigeration. The results demonstrated that the degree of protein oxidation increased with refrigeration time, and the consumption of these oxidized proteins may disrupt gut microbiota composition and increase the risk of chronic inflammation. Therefore, cooked rice and wheat steamed bread should be eaten immediately or kept refrigerated for as short a time as possible.
{"title":"Effects of refrigeration-induced protein oxidation of rice and wheat steamed bread on the human gut microbiota in an in vitro fermentation model","authors":"Qiong Wu ,&nbsp;Xiaojie Cui ,&nbsp;Yuhui Yang ,&nbsp;Keying Chu ,&nbsp;Ru Liu ,&nbsp;Sijin Gao ,&nbsp;Yanli Xie","doi":"10.1016/j.lwt.2025.117657","DOIUrl":"10.1016/j.lwt.2025.117657","url":null,"abstract":"<div><div>Rice and wheat steamed bread are common staple foods and important protein sources in the human diet. They are often prepared and refrigerated for later consumption. Here, we explored the influences of refrigeration on protein oxidation in rice and wheat steamed bread and investigated the effects of the resulting oxidized proteins on the human gut microbiota using an <em>in vitro</em> fermentation model. We found that as refrigeration time increased, the levels of protein oxidation products, including carbonyl groups and advanced glycation end products, in rice and wheat steamed bread increased, whereas those of free sulfhydryl and free amino groups decreased. The levels of specific amino acids (tyrosine, tryptophan, and glutamic acid) decreased with refrigeration, whereas those of amino acid oxidation products (dityrosine, <em>N′</em>-formylkynurenine, and kynurenine) increased. Furthermore, the relative abundance of potentially harmful bacteria, particularly <em>Sutterella</em> and <em>Tyzzerella,</em> increased, whereas that of probiotics, particularly <em>Bifidobacterium</em> and <em>Phascolarctobacterium</em>, decreased when rice and steamed bread proteins subjected to different refrigeration times were fermented with human gut microbiota. Moreover, the concentrations of short-chain fatty acids (acetate, propionate, and butyrate) in fermentation broth decreased with refrigeration. The results demonstrated that the degree of protein oxidation increased with refrigeration time, and the consumption of these oxidized proteins may disrupt gut microbiota composition and increase the risk of chronic inflammation. Therefore, cooked rice and wheat steamed bread should be eaten immediately or kept refrigerated for as short a time as possible.</div></div>","PeriodicalId":382,"journal":{"name":"LWT - Food Science and Technology","volume":"222 ","pages":"Article 117657"},"PeriodicalIF":6.0,"publicationDate":"2025-03-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143643190","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}
引用次数: 0
Fabrication, characterization, and application of soluble oat-soybean protein and oat-pea protein composites prepared using an alkaline-thermal treatment
IF 6 1区 农林科学 Q1 FOOD SCIENCE & TECHNOLOGY Pub Date : 2025-03-16 DOI: 10.1016/j.lwt.2025.117655
Qingmei Rao , Jun Chen , David Julian McClements , Qin Geng , Jialong Han , Lizhen Deng , Yihui Wang , Taotao Dai
Recently, combining two or more proteins to create a novel protein blend with a higher nutritional value and better functional properties than the individual proteins has become popular. In this study, oat-soy protein (OSP) and oat-pea protein (OPP) blends were prepared by combining oat protein isolate (OPI) with either soy protein isolate (SPI) or pea protein (PP) using an alkaline-thermal treatment. This treatment involving incubating the protein mixtures at pH 12 and 55 °C for 1.5 h, followed by cooling to ambient temperature and neutralization to pH 7. The water-solubility of the resulting OSP (95.2 %) and OPP (96.2 %) blends was relatively high. SDS-PAGE analysis indicated that no new subunits were formed in the protein blends. Circular dichroism and fluorescence spectroscopy showed that the proteins in the blends had a more flexible structure than the original proteins and had undergone some protein-protein interactions. The mean diameters of the particles in the OSP and OPP dispersions were 283 and 612 nm, while their ζ-potentials were −34 and −38 mV, respectively. Scanning electron microscopy showed that the proteins in the blends were uniformly dispersed throughout the dispersions. The analysis of the chemical showed that the formed of composite proteins during alkaline-thermal treatment was driven by hydrophobic reactions in main role. Compared to the individual proteins, the protein blends exhibited better thermal stability, lower interfacial tension, higher surface hydrophobicity, stronger emulsification ability, and more low molecular weight fraction. Taken together, the results showed that a simple alkaline-thermal treatment can be used to improve the solubility and functionality of protein blends.
{"title":"Fabrication, characterization, and application of soluble oat-soybean protein and oat-pea protein composites prepared using an alkaline-thermal treatment","authors":"Qingmei Rao ,&nbsp;Jun Chen ,&nbsp;David Julian McClements ,&nbsp;Qin Geng ,&nbsp;Jialong Han ,&nbsp;Lizhen Deng ,&nbsp;Yihui Wang ,&nbsp;Taotao Dai","doi":"10.1016/j.lwt.2025.117655","DOIUrl":"10.1016/j.lwt.2025.117655","url":null,"abstract":"<div><div>Recently, combining two or more proteins to create a novel protein blend with a higher nutritional value and better functional properties than the individual proteins has become popular. In this study, oat-soy protein (OSP) and oat-pea protein (OPP) blends were prepared by combining oat protein isolate (OPI) with either soy protein isolate (SPI) or pea protein (PP) using an alkaline-thermal treatment. This treatment involving incubating the protein mixtures at pH 12 and 55 °C for 1.5 h, followed by cooling to ambient temperature and neutralization to pH 7. The water-solubility of the resulting OSP (95.2 %) and OPP (96.2 %) blends was relatively high. SDS-PAGE analysis indicated that no new subunits were formed in the protein blends. Circular dichroism and fluorescence spectroscopy showed that the proteins in the blends had a more flexible structure than the original proteins and had undergone some protein-protein interactions. The mean diameters of the particles in the OSP and OPP dispersions were 283 and 612 nm, while their ζ-potentials were −34 and −38 mV, respectively. Scanning electron microscopy showed that the proteins in the blends were uniformly dispersed throughout the dispersions. The analysis of the chemical showed that the formed of composite proteins during alkaline-thermal treatment was driven by hydrophobic reactions in main role. Compared to the individual proteins, the protein blends exhibited better thermal stability, lower interfacial tension, higher surface hydrophobicity, stronger emulsification ability, and more low molecular weight fraction. Taken together, the results showed that a simple alkaline-thermal treatment can be used to improve the solubility and functionality of protein blends.</div></div>","PeriodicalId":382,"journal":{"name":"LWT - Food Science and Technology","volume":"222 ","pages":"Article 117655"},"PeriodicalIF":6.0,"publicationDate":"2025-03-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143643193","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}
引用次数: 0
Impact of ultrasound-assisted intermittent hydration during pumpkin seed germination on the structure, nutritional, bioactive, physical and techno-functional properties of flours
IF 6 1区 农林科学 Q1 FOOD SCIENCE & TECHNOLOGY Pub Date : 2025-03-15 DOI: 10.1016/j.lwt.2025.117654
Flaviana Coelho Pacheco , Irene Andressa , Ana Flávia Coelho Pacheco , Fábio Ribeiro dos Santos , Jeferson Silva Cunha , Nathalia de Andrade Neves , Raquel Guidetti Vendruscolo , Marcio Schmiele , Paulo Henrique Costa Paiva , Aline Artigiani Lima Tribst , Pedro Esteves Duarte Augusto , Bruno Ricardo de Castro Leite Júnior
This study investigated the ultrasound (US)-assisted intermittent hydration of pumpkin seeds (2 cycles of 10 min, at 25 or 45 °C, 38 W/L, 25 kHz), followed by germination (3 days, 25 °C), evaluating the structure, nutritional, bioactive, color, and techno-functional properties of the obtained flours. US-assisted hydration produced flours that were more porous and lighter in color. Germination reduced starch crystallinity (≤14.3 %) and altered the flour's aliphatic hydrocarbons, amino acids and carbohydrates, particularly in the C-H and C-O bonds, as evidenced by Fourier transform infrared (FTIR) spectroscopy. US treatment did not affect the flours' mineral nor fatty acid profiles. On the other hand, sonication effectively increased the content of gamma-aminobutyric acid (GABA) (15.6 % and 13.7 %) and the antioxidant activities, measured both by 2,2′-azino-bis (3-ethyl benzothiazoline-6-sulfonic acid) (ABTS) (29.4 % and 9.7 %) and 2,2-diphenyl-1-picrylhydrazyl (DPPH) (40.8 % and 2.4 %) methods compared to non-sonicated flours at 25 °C and 45 °C, respectively. US increased the water retention capacity, solubility index, foam capacity and foam stability by up to 49 %, 68 %, 143 % and 208 %, respectively. The enhanced nutritional and techno-functional properties suggest that germinated pumpkin seed flour hydrated under US, especially at 25 °C, is a promising and sustainable ingredient that can be used in products such as bread, cakes, cookies, and beverages.
{"title":"Impact of ultrasound-assisted intermittent hydration during pumpkin seed germination on the structure, nutritional, bioactive, physical and techno-functional properties of flours","authors":"Flaviana Coelho Pacheco ,&nbsp;Irene Andressa ,&nbsp;Ana Flávia Coelho Pacheco ,&nbsp;Fábio Ribeiro dos Santos ,&nbsp;Jeferson Silva Cunha ,&nbsp;Nathalia de Andrade Neves ,&nbsp;Raquel Guidetti Vendruscolo ,&nbsp;Marcio Schmiele ,&nbsp;Paulo Henrique Costa Paiva ,&nbsp;Aline Artigiani Lima Tribst ,&nbsp;Pedro Esteves Duarte Augusto ,&nbsp;Bruno Ricardo de Castro Leite Júnior","doi":"10.1016/j.lwt.2025.117654","DOIUrl":"10.1016/j.lwt.2025.117654","url":null,"abstract":"<div><div>This study investigated the ultrasound (US)-assisted intermittent hydration of pumpkin seeds (2 cycles of 10 min, at 25 or 45 °C, 38 W/L, 25 kHz), followed by germination (3 days, 25 °C), evaluating the structure, nutritional, bioactive, color, and techno-functional properties of the obtained flours. US-assisted hydration produced flours that were more porous and lighter in color. Germination reduced starch crystallinity (≤14.3 %) and altered the flour's aliphatic hydrocarbons, amino acids and carbohydrates, particularly in the C-H and C-O bonds, as evidenced by Fourier transform infrared (FTIR) spectroscopy. US treatment did not affect the flours' mineral nor fatty acid profiles. On the other hand, sonication effectively increased the content of gamma-aminobutyric acid (GABA) (15.6 % and 13.7 %) and the antioxidant activities, measured both by 2,2′-azino-bis (3-ethyl benzothiazoline-6-sulfonic acid) (ABTS) (29.4 % and 9.7 %) and 2,2-diphenyl-1-picrylhydrazyl (DPPH) (40.8 % and 2.4 %) methods compared to non-sonicated flours at 25 °C and 45 °C, respectively. US increased the water retention capacity, solubility index, foam capacity and foam stability by up to 49 %, 68 %, 143 % and 208 %, respectively. The enhanced nutritional and techno-functional properties suggest that germinated pumpkin seed flour hydrated under US, especially at 25 °C, is a promising and sustainable ingredient that can be used in products such as bread, cakes, cookies, and beverages.</div></div>","PeriodicalId":382,"journal":{"name":"LWT - Food Science and Technology","volume":"222 ","pages":"Article 117654"},"PeriodicalIF":6.0,"publicationDate":"2025-03-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143643194","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}
引用次数: 0
Effect of three fermentation methods on physicochemical and rheological characteristics of frozen dough
IF 6 1区 农林科学 Q1 FOOD SCIENCE & TECHNOLOGY Pub Date : 2025-03-14 DOI: 10.1016/j.lwt.2025.117651
Dongdong Xie, Xing Li, Jiaxin Zheng, Shuncheng Ren
The effect of three fermentation methods on frozen dough characteristics was explored by studying fermentation (50 min) and freezing (−18 °C, 5 days) (F-50), pre-fermentation (20 min), freezing (−18 °C, 5 days), and then re-fermentation (30 min) (F-20), freezing (−18 °C, 5 days) and fermentation (50 min) (F-0). F-50 had the lowest yeast survival, higher acidity, and higher glycerol content, resulting in increasing elasticity modulus and viscosity modulus. The F-50 had lower wet gluten content, higher content of loosely bound water, increased water mobility, and weakened -OH stretching vibration. The protein of F-50 had a more disordered secondary structure, with a higher disulfide (SS) and sulfhydryl (SH) bond content. F-20 dough had a higher ethanol content and ionic and hydrophobic bonds, resulting in lower elasticity and viscosity. The F-0 had higher yeast activity, lower acidity, higher wet gluten content, and more bound water content. F-0 also had an increased free sulfhydryl content, a reduced SS decreasing content, an increased content of ionic bonds, and stronger tensile properties. The F-0 method could ensure the sound quality of frozen fermented dough. Fermentation methods influenced the frozen dough properties by yeast activity, metabolic products, and water migration.
{"title":"Effect of three fermentation methods on physicochemical and rheological characteristics of frozen dough","authors":"Dongdong Xie,&nbsp;Xing Li,&nbsp;Jiaxin Zheng,&nbsp;Shuncheng Ren","doi":"10.1016/j.lwt.2025.117651","DOIUrl":"10.1016/j.lwt.2025.117651","url":null,"abstract":"<div><div>The effect of three fermentation methods on frozen dough characteristics was explored by studying fermentation (50 min) and freezing (−18 °C, 5 days) (F-50), pre-fermentation (20 min), freezing (−18 °C, 5 days), and then re-fermentation (30 min) (F-20), freezing (−18 °C, 5 days) and fermentation (50 min) (F-0). F-50 had the lowest yeast survival, higher acidity, and higher glycerol content, resulting in increasing elasticity modulus and viscosity modulus. The F-50 had lower wet gluten content, higher content of loosely bound water, increased water mobility, and weakened -OH stretching vibration. The protein of F-50 had a more disordered secondary structure, with a higher disulfide (SS) and sulfhydryl (SH) bond content. F-20 dough had a higher ethanol content and ionic and hydrophobic bonds, resulting in lower elasticity and viscosity. The F-0 had higher yeast activity, lower acidity, higher wet gluten content, and more bound water content. F-0 also had an increased free sulfhydryl content, a reduced SS decreasing content, an increased content of ionic bonds, and stronger tensile properties. The F-0 method could ensure the sound quality of frozen fermented dough. Fermentation methods influenced the frozen dough properties by yeast activity, metabolic products, and water migration.</div></div>","PeriodicalId":382,"journal":{"name":"LWT - Food Science and Technology","volume":"222 ","pages":"Article 117651"},"PeriodicalIF":6.0,"publicationDate":"2025-03-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143643181","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}
引用次数: 0
Peptide from tempeh-like fermented Chenopodium formosanum counters senescence while enhancing antioxidant ability in non-replicative aging
IF 6 1区 农林科学 Q1 FOOD SCIENCE & TECHNOLOGY Pub Date : 2025-03-13 DOI: 10.1016/j.lwt.2025.117641
Chen-Che Hsieh , Hui-Wen Lin , Hsiao-Chu Huang , Darin Khumsupan , Szu-Chuan Shen , Shin-Ping Lin , Chang-Wei Hsieh , Tsung-Yu Tsai , Sirima Suvarnakuta Jantama , Hsing-Chun Kuo , Kuan-Chen Cheng
The study assesses the protective effects of glycine-rich peptide (GRP) from tempeh-like fermented Chenopodium formosanum against non-replicative aging. By pretreating Hs68 cells with GRP and irradiating them with UVA, a reduction in oxidative stress was observed which positively contributed to cell survival rate. Moreover, transcriptomic analysis demonstrated that pretreatment with GRP prevents the downregulation of oxidative stress responses and an upregulated expression of cell cycle. Additionally, GRP was found to increase the expression of Nrf2 pathway while decreasing the expressions of p53 and p21. These findings were further investigated in Caenorhabditis elegans, where GRP treatment could extend lifespans and improve resistance to oxidative stress. Finally, molecular docking studies indicated GRP binds to the KEAP-BTB inhibitory site inhibitory site, potentially inhibiting activity of single O-linked β-N-acetylglucosamine transferase which facilitates activation of Nrf2 pathway. These results highlight the capability of GRP as a protective agent against oxidative stress and non-replicative aging.
{"title":"Peptide from tempeh-like fermented Chenopodium formosanum counters senescence while enhancing antioxidant ability in non-replicative aging","authors":"Chen-Che Hsieh ,&nbsp;Hui-Wen Lin ,&nbsp;Hsiao-Chu Huang ,&nbsp;Darin Khumsupan ,&nbsp;Szu-Chuan Shen ,&nbsp;Shin-Ping Lin ,&nbsp;Chang-Wei Hsieh ,&nbsp;Tsung-Yu Tsai ,&nbsp;Sirima Suvarnakuta Jantama ,&nbsp;Hsing-Chun Kuo ,&nbsp;Kuan-Chen Cheng","doi":"10.1016/j.lwt.2025.117641","DOIUrl":"10.1016/j.lwt.2025.117641","url":null,"abstract":"<div><div>The study assesses the protective effects of glycine-rich peptide (GRP) from tempeh-like fermented <em>Chenopodium formosanum</em> against non-replicative aging. By pretreating Hs68 cells with GRP and irradiating them with UVA, a reduction in oxidative stress was observed which positively contributed to cell survival rate. Moreover, transcriptomic analysis demonstrated that pretreatment with GRP prevents the downregulation of oxidative stress responses and an upregulated expression of cell cycle. Additionally, GRP was found to increase the expression of Nrf2 pathway while decreasing the expressions of <em>p53</em> and <em>p21</em>. These findings were further investigated in <em>Caenorhabditis elegans</em>, where GRP treatment could extend lifespans and improve resistance to oxidative stress. Finally, molecular docking studies indicated GRP binds to the KEAP-BTB inhibitory site inhibitory site, potentially inhibiting activity of single O-linked β-N-acetylglucosamine transferase which facilitates activation of Nrf2 pathway. These results highlight the capability of GRP as a protective agent against oxidative stress and non-replicative aging.</div></div>","PeriodicalId":382,"journal":{"name":"LWT - Food Science and Technology","volume":"222 ","pages":"Article 117641"},"PeriodicalIF":6.0,"publicationDate":"2025-03-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143642331","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}
引用次数: 0
Development of a protein-enriched oat beverage: Enhancing antioxidant activity, functional properties and stability with soy protein hydrolysates
IF 6 1区 农林科学 Q1 FOOD SCIENCE & TECHNOLOGY Pub Date : 2025-03-13 DOI: 10.1016/j.lwt.2025.117644
Antonella Luciana Grosso , Giulia Cestonaro , Matteo Scampicchio , Giovanna Ferrentino , Enrico Costanzo
Oat beverages are popular as dairy alternatives, but their low protein content limit their functionality. Soybean protein hydrolysates, derived from enzymatic hydrolysis, could improve both the nutritional and functional properties of these beverages. This study aimed to develop a protein-enriched oat beverage with enhanced functional and physical properties by incorporating soybean protein hydrolysates. Soybean protein hydrolysates were prepared from defatted soybean cake isolates. Oat beverages were enriched to 3 % protein concentration using either protein isolates or hydrolysates. The chemical composition, physical properties, antioxidant activity (ABTS and ORAC assay) and volatile profile (PTR-MS) of the prepared beverages were investigated. Hydrolysate-enriched beverages exhibited higher antioxidant activity (2848 ± 121 μmol TE/g) and phenolic content (1334 ± 25 μmol GAE/g) than isolate-enriched beverages. They also showed improved physical stability, with reduced sedimentation. The volatile profile of the hydrolysate beverage was similar to the control.
Soybean protein hydrolysates were effective for enhancing the nutritional and functional quality of oat-based beverages with potential for wider application in plant-based formulations.
{"title":"Development of a protein-enriched oat beverage: Enhancing antioxidant activity, functional properties and stability with soy protein hydrolysates","authors":"Antonella Luciana Grosso ,&nbsp;Giulia Cestonaro ,&nbsp;Matteo Scampicchio ,&nbsp;Giovanna Ferrentino ,&nbsp;Enrico Costanzo","doi":"10.1016/j.lwt.2025.117644","DOIUrl":"10.1016/j.lwt.2025.117644","url":null,"abstract":"<div><div>Oat beverages are popular as dairy alternatives, but their low protein content limit their functionality. Soybean protein hydrolysates, derived from enzymatic hydrolysis, could improve both the nutritional and functional properties of these beverages. This study aimed to develop a protein-enriched oat beverage with enhanced functional and physical properties by incorporating soybean protein hydrolysates. Soybean protein hydrolysates were prepared from defatted soybean cake isolates. Oat beverages were enriched to 3 % protein concentration using either protein isolates or hydrolysates. The chemical composition, physical properties, antioxidant activity (ABTS and ORAC assay) and volatile profile (PTR-MS) of the prepared beverages were investigated. Hydrolysate-enriched beverages exhibited higher antioxidant activity (2848 ± 121 μmol TE/g) and phenolic content (1334 ± 25 μmol GAE/g) than isolate-enriched beverages. They also showed improved physical stability, with reduced sedimentation. The volatile profile of the hydrolysate beverage was similar to the control.</div><div>Soybean protein hydrolysates were effective for enhancing the nutritional and functional quality of oat-based beverages with potential for wider application in plant-based formulations.</div></div>","PeriodicalId":382,"journal":{"name":"LWT - Food Science and Technology","volume":"222 ","pages":"Article 117644"},"PeriodicalIF":6.0,"publicationDate":"2025-03-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143631802","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}
引用次数: 0
Characterization of a novel bacteriophage PS1 targeting Bacillus licheniformis for biocontrol application in dairy products
IF 6 1区 农林科学 Q1 FOOD SCIENCE & TECHNOLOGY Pub Date : 2025-03-13 DOI: 10.1016/j.lwt.2025.117645
Minji Kim, Bokyung Son
Bacillus licheniformis, a major food spoilage bacterium, presents significant challenges to food safety due to its robust survival in harsh environments, its role in causing foodborne illnesses, and its negative impact on product shelf life. Current control methods like pasteurization and the use of antibiotics often compromise food quality and contribute to antibiotic resistance, highlighting the need for more effective strategies. In this study, a novel bacteriophage (phage), PS1, specifically infecting B. licheniformis was isolated from environmental samples. PS1 demonstrated a narrow host range, lysing only B. licheniformis strains among the various bacterial strains tested. Furthermore, lysis was maintained for at least 16 h post-infection at multiplicities of infection ranging from 1 to 0.0001 in vitro. The phage PS1 showed excellent stability in a wide range of pHs (pH 5–11), temperatures (4–65 °C), and NaCl concentrations (0–1000 mM). Bioinformatic analysis revealed that the genome of PS1 consists of a 48,817 bp double-stranded linear DNA with 71 open reading frames. Phage PS1 is predicted to lack genes associated with toxins, virulence factors, antibiotic resistance genes, or lysogeny-related elements, supporting its safety for food applications. Additionally, PS1 effectively inhibited the growth of B. licheniformis in milk for 24 h at room temperature (22–25 °C) and 30 °C. To our best knowledge, this is the first report demonstrating a lytic phage infecting B. licheniformis. These findings suggest that the novel phage PS1 could serve as an effective biological control agent and an alternative to antimicrobials for controlling B. licheniformis in dairy products.
{"title":"Characterization of a novel bacteriophage PS1 targeting Bacillus licheniformis for biocontrol application in dairy products","authors":"Minji Kim,&nbsp;Bokyung Son","doi":"10.1016/j.lwt.2025.117645","DOIUrl":"10.1016/j.lwt.2025.117645","url":null,"abstract":"<div><div><em>Bacillus licheniformis</em>, a major food spoilage bacterium, presents significant challenges to food safety due to its robust survival in harsh environments, its role in causing foodborne illnesses, and its negative impact on product shelf life. Current control methods like pasteurization and the use of antibiotics often compromise food quality and contribute to antibiotic resistance, highlighting the need for more effective strategies. In this study, a novel bacteriophage (phage), PS1, specifically infecting <em>B. licheniformis</em> was isolated from environmental samples. PS1 demonstrated a narrow host range, lysing only <em>B. licheniformis</em> strains among the various bacterial strains tested. Furthermore, lysis was maintained for at least 16 h post-infection at multiplicities of infection ranging from 1 to 0.0001 <em>in vitro</em>. The phage PS1 showed excellent stability in a wide range of pHs (pH 5–11), temperatures (4–65 °C), and NaCl concentrations (0–1000 mM). Bioinformatic analysis revealed that the genome of PS1 consists of a 48,817 bp double-stranded linear DNA with 71 open reading frames. Phage PS1 is predicted to lack genes associated with toxins, virulence factors, antibiotic resistance genes, or lysogeny-related elements, supporting its safety for food applications. Additionally, PS1 effectively inhibited the growth of <em>B. licheniformis</em> in milk for 24 h at room temperature (22–25 °C) and 30 °C. To our best knowledge, this is the first report demonstrating a lytic phage infecting <em>B. licheniformis</em>. These findings suggest that the novel phage PS1 could serve as an effective biological control agent and an alternative to antimicrobials for controlling <em>B. licheniformis</em> in dairy products.</div></div>","PeriodicalId":382,"journal":{"name":"LWT - Food Science and Technology","volume":"222 ","pages":"Article 117645"},"PeriodicalIF":6.0,"publicationDate":"2025-03-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143643191","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}
引用次数: 0
Characterization of a novel Salmonella enterica serovar Manhattan phage and its inhibitory effects in vitro and in food matrices
IF 6 1区 农林科学 Q1 FOOD SCIENCE & TECHNOLOGY Pub Date : 2025-03-13 DOI: 10.1016/j.lwt.2025.117617
Xiaojie Qin , Tingyu Liu , Jiayi Xue , Wei Zhang , Hanxuan Li , Yangtai Liu , Xiang Wang , Zhuosi Li , Yue Ma , Xuejuan Xia , Qingli Dong
Salmonella enterica serovar Manhattan (Salmonella Manhattan) is an important foodborne pathogen that poses a significant threat to food safety and public health. Phage biocontrol is increasingly being utilized as a natural and eco-friendly approach to reduce bacterial contamination in the food chain, but there have been no reports of phages targeting Salmonella Manhattan. In this study, a novel phage targeting Salmonella Manhattan, designated vB_Sal_M467, was successfully isolated and characterized. Phage vB_Sal_M467 was able to lyse 12 different antibiotic-resistant Salmonella serovars. Morphological and genomic analysis revealed that phage vB_Sal_M467 belonged to the class Caudovirales and the genus Kayfunavirus. The 40, 111 bp double-stranded DNA genome encoded lysis-associated proteins, including endopeptidase Rz, holin, and lysozyme, but lacked virulence factors, antibiotic resistance genes, RNA-coding elements (tRNA/rRNA). Phage vB_Sal_M467 was stable over a wide range of temperatures (−20 °C–50 °C) and pH levels (3–11), and possessed a large burst size of 158.83 PFU/cell. In vitro bacteriolytic assays confirmed that phage vB_Sal_M467 effectively inhibited bacterial growth. Notably, significant antibacterial efficacy of phage vB_Sal_M467 against Salmonella Manhattan was observed in lettuce, milk, and apple juice at different temperatures (4 °C, 10 °C, 25 °C). Collectively, these findings highlight the potential of phage vB_Sal_M467 as a novel antibacterial agent for enhancing food safety.
{"title":"Characterization of a novel Salmonella enterica serovar Manhattan phage and its inhibitory effects in vitro and in food matrices","authors":"Xiaojie Qin ,&nbsp;Tingyu Liu ,&nbsp;Jiayi Xue ,&nbsp;Wei Zhang ,&nbsp;Hanxuan Li ,&nbsp;Yangtai Liu ,&nbsp;Xiang Wang ,&nbsp;Zhuosi Li ,&nbsp;Yue Ma ,&nbsp;Xuejuan Xia ,&nbsp;Qingli Dong","doi":"10.1016/j.lwt.2025.117617","DOIUrl":"10.1016/j.lwt.2025.117617","url":null,"abstract":"<div><div><em>Salmonella enterica</em> serovar Manhattan (<em>Salmonella</em> Manhattan) is an important foodborne pathogen that poses a significant threat to food safety and public health. Phage biocontrol is increasingly being utilized as a natural and eco-friendly approach to reduce bacterial contamination in the food chain, but there have been no reports of phages targeting <em>Salmonella</em> Manhattan. In this study, a novel phage targeting <em>Salmonella</em> Manhattan, designated vB_Sal_M467, was successfully isolated and characterized. Phage vB_Sal_M467 was able to lyse 12 different antibiotic-resistant <em>Salmonella</em> serovars. Morphological and genomic analysis revealed that phage vB_Sal_M467 belonged to the class <em>Caudovirales</em> and the genus <em>Kayfunavirus</em>. The 40, 111 bp double-stranded DNA genome encoded lysis-associated proteins, including endopeptidase Rz, holin, and lysozyme, but lacked virulence factors, antibiotic resistance genes, RNA-coding elements (tRNA/rRNA). Phage vB_Sal_M467 was stable over a wide range of temperatures (−20 °C–50 °C) and pH levels (3–11), and possessed a large burst size of 158.83 PFU/cell. <em>In vitro</em> bacteriolytic assays confirmed that phage vB_Sal_M467 effectively inhibited bacterial growth. Notably, significant antibacterial efficacy of phage vB_Sal_M467 against <em>Salmonella</em> Manhattan was observed in lettuce, milk, and apple juice at different temperatures (4 °C, 10 °C, 25 °C). Collectively, these findings highlight the potential of phage vB_Sal_M467 as a novel antibacterial agent for enhancing food safety.</div></div>","PeriodicalId":382,"journal":{"name":"LWT - Food Science and Technology","volume":"222 ","pages":"Article 117617"},"PeriodicalIF":6.0,"publicationDate":"2025-03-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143637110","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}
引用次数: 0
Ultrasound-assisted protein extraction for deep proteome analysis of Spirulina and Chlorella microalgae
IF 6 1区 农林科学 Q1 FOOD SCIENCE & TECHNOLOGY Pub Date : 2025-03-12 DOI: 10.1016/j.lwt.2025.117647
Ludovica S. Guadalupi , Mariachiara Bianco , Tommaso R.I. Cataldi , Tine Ravnsborg , Ole N. Jensen , Cosima D. Calvano
Microalgae Spirulina (Arthrospira platensis) and Chlorella (Chlorella vulgaris) are gaining attention as sustainable alternative protein sources to address the needs of a growing global population. However, their tough cell walls present a significant challenge for efficient and more quantitative protein extraction. This study introduces a simple, cost-effective, and scalable "one-pot" protocol for extracting microalgal proteins by ultrasound-assisted methods in an aqueous buffer. The combination of ultrasonication and sodium deoxycholate successfully breaks down the resilient cell walls, improves protein solubility in water, and achieves high extraction yields of 81–86 %. This performance significantly surpasses traditional methods, such as Tris-HCl buffer (0.7–1.2 % yields) and chloroform/methanol solvent (4.5–14 % yields). Using this method, 1354 proteins were identified in Spirulina and 771 in Chlorella, each with over 10 % sequence coverage. This enabled the recovery of numerous bioactive peptides, including 161 candidates for Spirulina and 60 for Chlorella from phycobiliproteins, all comprising at least three amino acid residues. These peptides hold the potential for creating bioactive hydrolysates and functional ingredients for food and pharmaceutical applications, following detergent removal via appropriate purification. This optimized protocol offers a promising solution for large-scale, safe microalgae processing and facilitates the production of bioavailable peptides from microalgae species.
{"title":"Ultrasound-assisted protein extraction for deep proteome analysis of Spirulina and Chlorella microalgae","authors":"Ludovica S. Guadalupi ,&nbsp;Mariachiara Bianco ,&nbsp;Tommaso R.I. Cataldi ,&nbsp;Tine Ravnsborg ,&nbsp;Ole N. Jensen ,&nbsp;Cosima D. Calvano","doi":"10.1016/j.lwt.2025.117647","DOIUrl":"10.1016/j.lwt.2025.117647","url":null,"abstract":"<div><div>Microalgae Spirulina (<em>Arthrospira platensis</em>) and Chlorella (<em>Chlorella vulgaris</em>) are gaining attention as sustainable alternative protein sources to address the needs of a growing global population. However, their tough cell walls present a significant challenge for efficient and more quantitative protein extraction. This study introduces a simple, cost-effective, and scalable \"one-pot\" protocol for extracting microalgal proteins by ultrasound-assisted methods in an aqueous buffer. The combination of ultrasonication and sodium deoxycholate successfully breaks down the resilient cell walls, improves protein solubility in water, and achieves high extraction yields of 81–86 %. This performance significantly surpasses traditional methods, such as Tris-HCl buffer (0.7–1.2 % yields) and chloroform/methanol solvent (4.5–14 % yields). Using this method, 1354 proteins were identified in Spirulina and 771 in Chlorella, each with over 10 % sequence coverage. This enabled the recovery of numerous bioactive peptides, including 161 candidates for Spirulina and 60 for Chlorella from phycobiliproteins, all comprising at least three amino acid residues. These peptides hold the potential for creating bioactive hydrolysates and functional ingredients for food and pharmaceutical applications, following detergent removal <em>via</em> appropriate purification. This optimized protocol offers a promising solution for large-scale, safe microalgae processing and facilitates the production of bioavailable peptides from microalgae species.</div></div>","PeriodicalId":382,"journal":{"name":"LWT - Food Science and Technology","volume":"222 ","pages":"Article 117647"},"PeriodicalIF":6.0,"publicationDate":"2025-03-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143643192","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}
引用次数: 0
A crude, alginate-rich product from Alaria esculenta and Saccharina latissima – process development and exploration as texture ingredient
IF 6 1区 农林科学 Q1 FOOD SCIENCE & TECHNOLOGY Pub Date : 2025-03-12 DOI: 10.1016/j.lwt.2025.117643
Johanna Liberg Krook , Turid Rustad , Tore Kristoffer Wæhre , Anne Mari Langeng , Inga Marie Aasen , Finn Lillelund Aachmann
Development of functional ingredients from cultivated brown seaweed may promote broader use in food products and meet a growing demand for cleaner labels. This study presents a simple, cost-effective method to produce a crude alginate-rich product from Saccharina latissima and Alaria esculenta. Instead of extracting alginate, the process retains it within the seaweed matrix by washing the biomass at low pH to release crosslinking ions, followed by neutralization to convert alginic acid into Na- or K-alginate. Gelation could be controlled by reintroduction of Ca2+. Through demineralisation, alginate junction zones were exposed and made available for crosslinking when Ca2+ was reintroduced. Hydrogels prepared from acid-washed products demonstrated similar strength to gels from Laminaria hyperborea stipe alginate. The gels were elastic and synergetic (37.2–48.6 %), attributed to more MG sequences and low alginate concentrations (<5 g/L). A correlation was observed between reduced Ca content after treatment and increasing gel strength. To explore clean-label ingredient alternatives and increase consumer acceptability, selected products were tested as binders in plant-based patties. The patties were easily shapable and held structure during cooking but had less hardness, springiness, and cohesiveness than a commercial patty with methylcellulose as binder. However, low cooking losses demonstrated high water-holding capacity of acid-washed products.
从栽培褐海藻中开发功能性配料可促进食品的更广泛应用,并满足对更清洁标签日益增长的需求。本研究提出了一种简单、经济高效的方法,用于从 Saccharina latissima 和 Alaria esculenta 中生产富含粗海藻酸盐的产品。该方法不提取海藻酸,而是通过在低 pH 值条件下洗涤生物质以释放交联离子,然后中和将海藻酸转化为 Na- 或 K-海藻酸,从而将海藻酸保留在海藻基质中。可通过重新引入 Ca2+ 来控制凝胶化。通过脱矿化作用,藻酸交界区暴露出来,在重新引入 Ca2+ 时可用于交联。用酸洗产品制备的水凝胶的强度与用海藻酸层叠管制备的凝胶相似。凝胶具有弹性和协同性(37.2-48.6%),这归因于更多的 MG 序列和较低的海藻酸浓度(<5 g/L)。处理后钙含量降低与凝胶强度增加之间存在相关性。为了探索清洁标签配料替代品并提高消费者的接受度,对选定产品作为植物基肉饼的粘合剂进行了测试。与使用甲基纤维素作为粘合剂的商业肉饼相比,这些肉饼在烹饪过程中容易成型并保持结构,但硬度、弹性和凝聚力较差。不过,低烹饪损失表明酸洗产品具有很高的保水能力。
{"title":"A crude, alginate-rich product from Alaria esculenta and Saccharina latissima – process development and exploration as texture ingredient","authors":"Johanna Liberg Krook ,&nbsp;Turid Rustad ,&nbsp;Tore Kristoffer Wæhre ,&nbsp;Anne Mari Langeng ,&nbsp;Inga Marie Aasen ,&nbsp;Finn Lillelund Aachmann","doi":"10.1016/j.lwt.2025.117643","DOIUrl":"10.1016/j.lwt.2025.117643","url":null,"abstract":"<div><div>Development of functional ingredients from cultivated brown seaweed may promote broader use in food products and meet a growing demand for cleaner labels. This study presents a simple, cost-effective method to produce a crude alginate-rich product from <em>Saccharina latissima</em> and <em>Alaria esculenta</em>. Instead of extracting alginate, the process retains it within the seaweed matrix by washing the biomass at low pH to release crosslinking ions, followed by neutralization to convert alginic acid into Na- or K-alginate. Gelation could be controlled by reintroduction of Ca<sup>2+</sup>. Through demineralisation, alginate junction zones were exposed and made available for crosslinking when Ca<sup>2+</sup> was reintroduced. Hydrogels prepared from acid-washed products demonstrated similar strength to gels from <em>Laminaria hyperborea</em> stipe alginate. The gels were elastic and synergetic (37.2–48.6 %), attributed to more MG sequences and low alginate concentrations (&lt;5 g/L). A correlation was observed between reduced Ca content after treatment and increasing gel strength. To explore clean-label ingredient alternatives and increase consumer acceptability, selected products were tested as binders in plant-based patties. The patties were easily shapable and held structure during cooking but had less hardness, springiness, and cohesiveness than a commercial patty with methylcellulose as binder. However, low cooking losses demonstrated high water-holding capacity of acid-washed products.</div></div>","PeriodicalId":382,"journal":{"name":"LWT - Food Science and Technology","volume":"222 ","pages":"Article 117643"},"PeriodicalIF":6.0,"publicationDate":"2025-03-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143628494","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}
引用次数: 0
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LWT - Food Science and Technology
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