Food Hydrocolloids最新文献

{"title":"Heat-induced dissociation and association of proteins in hempseed protein bodies","authors":"Duc Toan Do,&nbsp;Aiqian Ye,&nbsp;Harjinder Singh,&nbsp;Alejandra Acevedo-Fani","doi":"10.1016/j.foodhyd.2025.111372","DOIUrl":"10.1016/j.foodhyd.2025.111372","url":null,"abstract":"<div><div>Protein bodies (PBs) are naturally occurring storage organelles in seeds. In hempseeds, the major storage proteins, including edestin (11S globulin) and albumin, are primarily located in the crystalloids and proteinaceous matrices of hemp protein bodies (HPBs), respectively. The retention of native PB structures in flours and dry-fractionated protein ingredients has important implications for protein functionality and digestibility, especially when heat treatment is applied during processing. While the thermal behaviour of hempseed proteins has been studied in protein isolate systems, to the best of our knowledge, it has not yet been explored in HPB systems. In this study, we isolated native HPBs using an enzymatic method. Aqueous suspensions of HPBs (4 % protein, w/w) were heated at selected temperatures (60–100 °C) and pH 7 for 20 min, followed by hydrolysis with trypsin at pH 7 and 37 °C for 120 min. The thermal aggregation of proteins in HPBs was characterised using confocal laser scanning microscopy (CLSM) and sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). The hydrolysis of HPBs by trypsin was monitored over 120 min by measuring the degree of protein hydrolysis (DH) and analysing SDS-PAGE. Aggregation of edestin in HPBs, primarily driven by disulfide bond formation, occurred upon heating, most noticeably at temperatures above 80 °C. Heating increased DH and altered protein degradation patterns of both acidic and basic subunits of edestin. This may be related to conformational changes in the HPB structure resulting from heat-induced dissociation-association of multiple HPB protein fractions, including 11S edestin, 7S globulin, and 2S albumin. These findings contribute to our understanding of the structure-hydrolysis relationships of HPBs, potentially leading to their use as a new plant-based material for food applications.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"166 ","pages":"Article 111372"},"PeriodicalIF":11.0,"publicationDate":"2025-03-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143706261","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}

{"title":"Conjugation of flaxseed protein and plant polysaccharides: Process optimization, structural characterization and technical-function evaluation","authors":"Ziqin Ye ,&nbsp;Shengrui Gan ,&nbsp;Jinying Wang,&nbsp;Furong Yang,&nbsp;Guoxin Dong","doi":"10.1016/j.foodhyd.2025.111371","DOIUrl":"10.1016/j.foodhyd.2025.111371","url":null,"abstract":"<div><div>In this study, the covalent conjugation conditions of flaxseed protein isolate (FPI) with flaxseed gum (FG), oat β-glucan (BG), and soybean polysaccharide (SP) were optimized separately using the ultrasound-assisted (U) method. The effects of the conjugation on the structure, function, and antioxidant properties of FPI were explored based on the optimal conditions. The results showed that the infrared absorption peaks of FPI in each sample changed and shifted in amide I and II bands after conjugation, indicating the progression of the Maillard reaction. Fluorescence intensity decreased and red-shifted emission peaks (10–15 nm), suggesting increased protein unfolding and improved hydrophilic interactions. Moreover, conjugation decreased the intensity of the UV absorption peaks, with the maximum absorption shifting to shorter wavelengths. Further validated the structural modifications associated with the Maillard reaction. Ultrasound-assisted conjugation also improved the functional properties in all samples, especially FPI-FG-U showed the best foaming capacity (improved to 80.39 %) and emulsification activity and stability (increased to 64.95 m²/g and 51.80 %), confirmed the correlation between structural changes and functional improvements. ABTS⁺ and DPPH radical scavenging experiments showed that the antioxidant capacity of FPI was enhanced by covalent conjugation. This study shows that the functional performance of FPI can be extended by covalently linking a combination of sonication, thus broadening their potential uses in the food sector and beyond.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"166 ","pages":"Article 111371"},"PeriodicalIF":11.0,"publicationDate":"2025-03-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143706259","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}

{"title":"Improving rheology and 3D printability of pea, fava and mung bean proteins with raw and fermented millet flour","authors":"Saphal Ghimire ,&nbsp;Muhammad Umar ,&nbsp;Chaiwut Gamonpilas ,&nbsp;Anil Kumar Anal","doi":"10.1016/j.foodhyd.2025.111369","DOIUrl":"10.1016/j.foodhyd.2025.111369","url":null,"abstract":"<div><div>This study aims to enhance the rheological, 3D printing, textural, and nutritional properties of meat analogs by adding the raw and fermented finger millet (RFM and FFM) flour in pea, fava, and mung bean protein isolates (PPI, FPI, and MPI). The gel strength of all samples increased significantly by increasing the protein concentration. The tanδ values for all samples were below 1 (0.16–0.26) indicating elastic and solid-like behavior (G’ &gt; G″). Frequency index increased for FPI (0.09–0.12), PPI (0.10–0.12), and MPI (from 0.10 to 0.13 for) based samples containing both RFM and FFM. The yield stress increased for FPR (111.34–128.47 Pa), FPF (122.73–132.1 Pa), PPR (93.37–166.39 Pa), PPF (126.31–180.4 Pa), MPR (46.17–162.93 Pa), MPF (86.12–189.28 Pa). The optimal formulation in terms of printing, smoothness, texture, and post-processing design retention for all protein-based inks was at finger millet flour to protein ratio of 1:4. However, the MPI-based samples exhibited superior characteristics of elasticity, shear thinning behavior, printing performance, frying stability, and texture. The structural analysis confirmed the higher interactions between FFM flour and proteins, enhancing rheological and textural properties. The protein digestibility values of the analogs ranged from 81.8 % to 91.2 %, with MPI samples exhibiting the highest protein digestibility. This research highlights the potential of utilizing lesser-known cereals to create edible and nutritious analogs through 3D printing.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"166 ","pages":"Article 111369"},"PeriodicalIF":11.0,"publicationDate":"2025-03-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143682578","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}

{"title":"Improving the physicochemical properties of microbial transglutaminase-induced fish gelatin gels by incorporating sanxan as a novel way","authors":"Kangning Wang,&nbsp;Yiyang Jia,&nbsp;Xin Meng,&nbsp;Jiayi Hou,&nbsp;Fuping Lu,&nbsp;Yihan Liu","doi":"10.1016/j.foodhyd.2025.111370","DOIUrl":"10.1016/j.foodhyd.2025.111370","url":null,"abstract":"<div><div>Fish gelatin (FG) is recognized as a promising alternative to mammalian gelatin sources. However, some undesirable physicochemical properties of FG such as weak texture, poor rheology, and poor thermostability limit its application. This study explored the effect of sanxan (SX) on the FG gelling behavior under conditions induced by microbial transglutaminase (MTGase). It was observed that the water-holding capacity, gel strength, and viscoelastic characteristics of FG gel were enhanced by adding SX. Meanwhile, thermogravimetric analysis exhibited that the thermostability of FG was also improved. Zeta potential measurements suggested the presence of electrostatic interactions between SX and FG. FTIR spectral analysis revealed that the added SX significantly affected the secondary structure of FG and verified the presence of both hydrogen bond and electrostatic interactions between FG and SX. The added SX reduced the α-helix content and increased the β-sheet content, leading to orderly aggregation and protein unfolding. This resulted in the formation of a dense and uniform FG-SX composite gel network. Additionally, intrinsic fluorescence, surface hydrophobicity, and protein solubility analyses revealed that hydrophobic interactions are crucial in the forming the FG-SX composite gel. These findings offer new insights into the potential of SX as a natural and innovative gel modifier to enhance the functionality of enzyme-induced protein gel-based foods.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"166 ","pages":"Article 111370"},"PeriodicalIF":11.0,"publicationDate":"2025-03-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143706257","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}

{"title":"Ultrasound-assisted phosphorylation on the functional and structural properties of fish gelatin","authors":"Qingfang Ying ,&nbsp;Bin Hu ,&nbsp;Yijia Li ,&nbsp;Liangying Xu ,&nbsp;Wenge Yang ,&nbsp;Shengnan Zhan ,&nbsp;Changrong Ou ,&nbsp;Tao Huang","doi":"10.1016/j.foodhyd.2025.111364","DOIUrl":"10.1016/j.foodhyd.2025.111364","url":null,"abstract":"<div><div>This study investigates the variations in ultrasound power and temperature of ultrasound-assisted phosphorylation (UAP) on the functional and structural properties of fish gelatin (FG). The results indicate that UAP significantly enhances the gel strength, antioxidant activity, and emulsifying properties of FG. FTIR analysis reveals structural changes, indicating that increased degrees of phosphorylation are associated with characteristic vibrational bands. Mass spectrometry identified phosphorylation sites in fish gelatin, primarily serine (Ser) and threonine (Thr), while molecular docking further revealed the major binding sites of these sites to sodium pyrophosphate. The study establishes that controlled ultrasound treatment, when combined with phosphorylation effectively improves FG properties, making it suitable for applications in the food and pharmaceutical industries.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"166 ","pages":"Article 111364"},"PeriodicalIF":11.0,"publicationDate":"2025-03-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143682515","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}

{"title":"Novel imine dynamic response films with grafting phenylalanine onto oxidized starch/pectin matrixes and regulated physiological metabolism of cherry tomatoes","authors":"Shuo Mao,&nbsp;Jiaying Zhang,&nbsp;Yingjie Xu,&nbsp;Qiao Wu,&nbsp;Tiehua Zhang,&nbsp;Chengwen Lu","doi":"10.1016/j.foodhyd.2025.111353","DOIUrl":"10.1016/j.foodhyd.2025.111353","url":null,"abstract":"<div><div>Dynamic response films with efficient, accurate and biodegradable properties greatly contribute to food packaging materials. In this study, phenylalanine was innovatively reversibly grafted onto oxidized starch via imine bonding and blended with Ca²⁺ and pectin to prepare novel imine dynamic responsive composite films (PO-PE/Ca). The results indicated that the cross-linking and dense structure formed by electrostatic interaction in PO-PE/Ca, and showed excellent thermal stability. The composite films displayed excellent mechanical property (elasticity modulus over 2100 MPa), and the water vapor permeability was 26.4 % lower than that of individual starch films. Additionally, the introduction of benzene rings and imine bonds significantly improved the ultraviolet shielding properties and transparency of the films. The internal imine bonds of PO-PE/Ca could be stimulated by acidic gases of fruit respiration, and constantly released phenylalanine to regulate fruit metabolism. The films effectively maintained fruit quality and significantly promoted phenol content (9.5 mg/100g) of fruits, showing resistance to <em>Botrytis cinerea</em> of cherry tomatoes during 10 d storage. This study provided a novel strategy for the development of dynamic controlled release packaging materials in food preservation.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"166 ","pages":"Article 111353"},"PeriodicalIF":11.0,"publicationDate":"2025-03-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143706258","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}

{"title":"Ultrasound-assisted construction of the curdlan-pea protein gel network for dysphagia management: Texture modification and interaction exploration","authors":"Huajian Xu ,&nbsp;Yunhao Lv ,&nbsp;Boxiang Zhou ,&nbsp;Xu Zhou ,&nbsp;Junwei Gao ,&nbsp;Dongling Qiao ,&nbsp;Bowen Li ,&nbsp;Binjia Zhang","doi":"10.1016/j.foodhyd.2025.111363","DOIUrl":"10.1016/j.foodhyd.2025.111363","url":null,"abstract":"<div><div>With the advancement of world population aging, dysphagia has become a pressing health challenge. Providing texture-improved foods is an effective strategy to reduce risk during eating for patients with dysphagia. In this study, the gel quality of pea protein isolate was effectively improved by curdlan gum combined with ultrasonic treatment, and it could be swallowed safely. Curdlan and/or ultrasound could improve the strength and water-holding capacity of pea protein isolate gel and increase the proportion of immobilized water. It was observed that ultrasound reduced the particle size of pea protein isolate in the sol, which might be beneficial for the interaction between protein and water, as well as the unfolding and cross-linking of the protein. In addition, ultrasound and/or curdlan promoted the formation of the uniform and dense gel structure by affecting the sol-gel transition process and modifying the protein conformation. In this regard, molecular dynamics simulation revealed that curdlan and pea protein molecules could be crosslinked through non-covalent interactions such as hydrogen bonding, van der Waals forces, and electrostatic forces, thus forming a stable three-dimensional network. The modified gels had good swallowing properties and were assessed as levels 5<strong>–</strong>6 according to the International Dysphagia Diet Standardization Initiative framework. Overall, ultrasound and curdlan are promising approaches for improving the quality of pea protein isolate gel. This study provides a new perspective on the precise regulation of gel food texture, which is valuable for the design of texture-improved food for elderly patients with dysphagia.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"166 ","pages":"Article 111363"},"PeriodicalIF":11.0,"publicationDate":"2025-03-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143734516","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}

{"title":"The molecular size and water dynamics effects of polyethylene glycol on starch gelatinization properties","authors":"Travest J. Woodbury,&nbsp;Lisa J. Mauer","doi":"10.1016/j.foodhyd.2025.111358","DOIUrl":"10.1016/j.foodhyd.2025.111358","url":null,"abstract":"<div><div>The mechanisms by which molecules influence the gelatinization temperature (T_gel) of starch are of both scientific and practical interest, since gelatinization affects the structure, texture, and functionality of starch-containing food and industrial applications. This study was designed to understand how polyethylene glycol (PEG, chosen for its unique physicochemical properties and pure size fractions) affects the gelatinization parameters of normal amylose-containing starches from four botanical sources (wheat, corn, tapioca, and potato) with differing amylopectin fine structures. Sucrose was also studied, since it is more effective at antiplasticizing starch, exhibited by higher T_gels, than many other small molecules which has posed challenges for reducing added sugars in foods. Differential scanning calorimetry was used to measure starch gelatinization in water and 15–45 % w/w solutions of sucrose and PEG molecules ranging in size from 200 to 10,000 g/mol. Solution density, water activity, and dynamic viscosity were also measured, and samples were viewed by confocal image analysis. The T_gels of all starch types were higher in 45 % w/w solutions of all PEGs, regardless of size, than of sucrose. Smaller PEGs (&lt;1000 g/mol, the size exclusion limit of starch granules) increased the T_gel more than the larger PEGs across all starch types and concentrations. Starch structural differences were associated with different extents of T_gel variations and ranges, with cereal starches exhibiting greater variation in the presence of PEG. Smaller PEG resulted in higher T_gels attributed to diffusion into starch granules and resultant stabilization via intermolecular hydrogen bonding. Larger PEG exerted effects on T_gel, even though they were too large to enter the starch granules, by limiting solvent plasticization. The findings highlight how PEGs of different sizes are more effective antiplasticizers of starch than sucrose and elucidate how additive molecular size dictates the gelatinization behavior and, by extension, the end-use properties of starch in food and non-food systems.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"166 ","pages":"Article 111358"},"PeriodicalIF":11.0,"publicationDate":"2025-03-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143706262","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}

{"title":"Exploration of interaction mechanisms and functional properties of coffee flavonoids and β-casein via multispectroscopy and molecular dynamics simulation","authors":"Jiyue Zhang ,&nbsp;Xiaoyu Zhai ,&nbsp;Xinxin Yu ,&nbsp;Minghua Qiu ,&nbsp;Rongsuo Hu ,&nbsp;Wenjiang Dong","doi":"10.1016/j.foodhyd.2025.111359","DOIUrl":"10.1016/j.foodhyd.2025.111359","url":null,"abstract":"<div><div>Milk coffee, a commonly consumed beverage, is prepared by mixing milk and coffee, which results in various interactions among their components. This study was aimed at investigating the interaction mechanisms of four coffee flavonoids (namely apigenin [AG], luteolin [LUT], quercetin [QC], and epigallocatechin gallate [EGCG]) and milk-derived β-casein (β-CN). Notably, LUT and QC bound to β-CN mostly via hydrogen bonds and van der Waals forces, whereas AG and EGCG primarily bound to β-CN via hydrophobic interactions. The trend of energy transfer efficiencies of the β-CN-flavonoid complex was as follows: β-CN-QC (50.20 %) &gt; β-CN-LUT (43.68 %) &gt; β-CN-EGCG (40.82 %) &gt; β-CN-AG (35.34 %). Additionally, the dynamic behavior of the β-CN-flavonoid interaction and structural alterations in the protein were validated by molecular dynamics (MD) simulations. Multispectroscopy results revealed flavonoid-mediated alterations in the secondary structure of β-CN, including increased amounts of random coil structure and a decrease in the proportion of α-helix, which resulted in a more open and loose protein structure. The noncovalent interactions between flavonoids and β-CN lead to decreased protein surface hydrophobicity, increased solubility, improved emulsifying activity, albeit with decreased emulsifying stability, and improved foaming ability and foam stability. Furthermore, the complex exhibited a superior antioxidant activity to that of either protein or flavonoid alone, suggesting the synergistic action of the compounds on the antioxidant activity. Altogether, our results of this study offer a theoretical foundation for comprehending the interaction mechanisms among coffee polyphenols and milk proteins for the creation of a functional beverage such as milk coffee.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"166 ","pages":"Article 111359"},"PeriodicalIF":11.0,"publicationDate":"2025-03-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143682516","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}

{"title":"Oil-based micro-sized extraction system designed from O/W Pickering emulsion template for highly efficient nanoplastics removal in the gastrointestinal tract","authors":"Xiao Fu ,&nbsp;Chi Zhang ,&nbsp;Xiao Tong Lu ,&nbsp;Fang Xiao Guo ,&nbsp;Xu Zhang ,&nbsp;Huixia Zhou ,&nbsp;Xin-Ai Guo ,&nbsp;Xiaoyu Wang ,&nbsp;Ching Yuan Hu ,&nbsp;Shuai Zhang ,&nbsp;Yong Hong Meng","doi":"10.1016/j.foodhyd.2025.111366","DOIUrl":"10.1016/j.foodhyd.2025.111366","url":null,"abstract":"<div><div>The widespread presence of nano-sized plastic particles in the environment and foods, and their potential harmful effects on human health through intestinal absorption, have become an escalating global concern. Current methods and technologies have limited focus on the removal of nanoplastics (NPs) from the human body. In this work, highly bio-safe natural oil droplets, covered by the interworking natural regenerated apple nanofibers (ANFs), demonstrated high efficacy in removing NPs from the gastrointestinal tract. Pectin-containing ANFs with native dissociated carboxyl groups act as stabilizers to produce a clean-label oil-in-water Pickering emulsions (O/W PE) together with canola oil and water. Attributing to the internetwork of ANFs, oil droplets are protected from shedding, and unabsorbed ANFs fabricated entangled networks ensure the distribution and stability of O/W PE in simulated gastrointestinal fluids. Notably, the extraction efficiency of NPs reached up to 100 % and 98.69 % in the simulated gastric and intestinal fluids, respectively. Additionally, the highly efficient O/W PE showed superior capability in removing NPs adhered to the small intestine. This study represents the first attempt to remove NPs from the gastrointestinal tract, offering an attractive and promising strategy for eliminating NPs from the human body.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"166 ","pages":"Article 111366"},"PeriodicalIF":11.0,"publicationDate":"2025-03-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143724264","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}