Food Hydrocolloids最新文献

{"title":"The competition between endogenous phospholipids and proteins from pea protein isolate rules their interfacial properties","authors":"Eléna Keuleyan ,&nbsp;Jeanne Kergomard ,&nbsp;Adeline Boire ,&nbsp;Elisabeth David-Briand ,&nbsp;Véronique Vié ,&nbsp;Anne Meynier ,&nbsp;Alain Riaublanc ,&nbsp;Claire Berton-Carabin","doi":"10.1016/j.foodhyd.2025.111475","DOIUrl":"10.1016/j.foodhyd.2025.111475","url":null,"abstract":"<div><div>Sustainable incentives foster the use of plant-based ingredients as emulsifiers, but their composition, functionality and interfacial properties deserve more attention. A recent study highlighted high contents of endogenous phospholipids in pea protein isolate (PPI) and the potential of high-pressure homogenization (HPH) to release submicron lipid structures in aqueous suspensions. These findings raised the pivotal question of the interfacial properties of this widespread ingredient, suggesting a competition between proteins and phospholipids for interfacial adsorption. Dilatational interfacial rheology measurements were conducted using either the soluble fraction of the ingredient as such, lipids extracted from PPI, or purified pea proteins (7S). Oscillatory deformations of the oil-water interfacial layers were analyzed using Lissajous plots, which substantiated the interactions between proteins and lipids by deciphering their respective contributions. The formation of mixed interfacial films according to the protein-to-lipid ratio was demonstrated, with a prevalent influence of pea lipids on the rheological signature of the films. Atomic force microscopy confirmed the formation of mixed interfacial films where lipid domains coexist with protein aggregates. These insights advance the current knowledge regarding the complexity and functionality of plant protein ingredients, which is important to promote the rational formulation of plant-based food products.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"168 ","pages":"Article 111475"},"PeriodicalIF":11.0,"publicationDate":"2025-04-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143887883","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":"Calcium-induced pea protein gels: Effect of structure on in-vitro protein digestibility and calcium bioaccessibility","authors":"Wenbo Ren ,&nbsp;Sarah H.E. Verkempinck ,&nbsp;Deniz Z. Gunes ,&nbsp;Tara Grauwet ,&nbsp;Lilia Ahrné","doi":"10.1016/j.foodhyd.2025.111478","DOIUrl":"10.1016/j.foodhyd.2025.111478","url":null,"abstract":"<div><div>The importance of plant protein gelation on the nutritional properties of foods is gaining considerable interest. In this study, we hypothesized that differences in the structural properties of calcium-induced pea protein gels would influence the <em>in vitro</em> protein digestibility and calcium bioaccessibility. These gels were created under different heating conditions (45 °C, 1000 min or 95 °C,10 min) and calcium concentrations (20 mM or 100 mM). The structural characteristics of gels showed that, within the testing range of this study, the influence of calcium concentration is more pronounced than that of the heating conditions. Gels with 20 mM calcium concentration had higher storage modulus Gʹ and also a finer, uniform gel network. Contrarily, the microstructure of gels formed at higher calcium concentration (100 mM) exhibited concentrated protein aggregates that shared fragile bonds. During the <em>in vitro</em> gastrointestinal digestion process, the heterogeneous gel network and compact aggregates in 100 mM gels seemed to limit the enzyme action, slowing the hydrolysis rate and resulting in a lower degree of protein hydrolysis. However, higher amounts of calcium in 100 mM gels resulted in higher levels of ionic calcium and soluble calcium, leading to higher calcium bioaccessibility. Interestingly, the bioaccessibility of calcium can be affected by protein hydrolysis due to the interaction between calcium ions and the released peptides. Thus, in the range of 20–100 mM calcium concentration, G′ correlates positively with the degree of proteolysis and negatively with calcium bioaccessibility.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"168 ","pages":"Article 111478"},"PeriodicalIF":11.0,"publicationDate":"2025-04-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143887273","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":"A green nanocoating approach to Lactobacillus plantarum using tea residue-derived phenolic compounds and cellulose nanocrystals","authors":"Ji-Hwan Lim ,&nbsp;Gyumi Na ,&nbsp;Jun-Won Kang","doi":"10.1016/j.foodhyd.2025.111469","DOIUrl":"10.1016/j.foodhyd.2025.111469","url":null,"abstract":"<div><div>Nanocoating technologies effectively enhance the stability and functionality of probiotics, overcoming challenges in their delivery and survival through the gastrointestinal tract. This study introduces a nanocoating method incorporating phenolic compounds and cellulose nanocrystals (CNCs) from green tea residues, aimed at improving the performance of <em>Lactobacillus plantarum</em> (LP). A cell-mediated catalytic single-cell coating process was developed, to optimize the formation of a polymeric phenolic layer and facilitating CNC adhesion, while preserving bacterial viability and growth. The coated LP showed improved tolerance to simulated gastric fluid and bile salts, and maintained significantly higher viability under oxidative stress. In a Caco-2 cell model exposed to H₂O₂, the phenolic-coated LP significantly improved cell viability compared to pristine LP, confirming its antioxidant efficacy. Furthermore, CNC incorporation increased the mucoadhesive properties of coated LP, as evidenced by in vitro and ex vivo assays. This study highlights the potential of repurposing green tea byproducts to develop sustainable and multifunctional nanocoatings. By improving probiotic survival, antioxidant activity, and mucosal adhesion, this sustainable approach presents a promising advancement in probiotic delivery systems.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"167 ","pages":"Article 111469"},"PeriodicalIF":11.0,"publicationDate":"2025-04-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143858783","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":"Emulsion gels structured with clementine pomace: a clean-label strategy for fat reduction","authors":"Joana Martínez-Martí ,&nbsp;Teresa Sanz ,&nbsp;Isabel Hernando ,&nbsp;Amparo Quiles","doi":"10.1016/j.foodhyd.2025.111471","DOIUrl":"10.1016/j.foodhyd.2025.111471","url":null,"abstract":"<div><div>The mounting demand for healthier and more sustainable food formulations, in conjunction with the World Health Organization's (WHO) guidelines recommending a maximum intake of saturated fat equivalent to 10 % of daily calories, has precipitated the exploration of alternatives to conventional plastic fat, which has been shown to effectively substitute structured fats while concomitantly contributing to a reduction in the overall fat content. In this study, emulsion gels were developed using physically treated clementine pomace (freeze-dried, extruded, and homogenized) as a clean-label structuring agent that is rich in hydrocolloids (polysaccharides and proteins). The study's objective was to assess the impact of pomace treatment, concentration (5 %–6 %), and oil content (40 %–50 %) on the microstructure, rheological properties, bioactive compound content, and physical and oxidative stability of the emulsion gels. The analysis revealed that freeze-dried pomace resulted in the most physically stable gels, as evidenced by microstructural and oil loss analyses. Emulsion gels with homogenized pomace exhibited robust solid-like behavior and augmented viscoelasticity, particularly at 40 % oil content. Regarding bioactive compounds, extrusion resulted in an increase in the total phenolic content and antioxidant capacity, whereas freeze-drying preserved a greater proportion of carotenoids. The oxidative stability assessment indicated that most emulsion gels retained peroxide values below the established legal limits after a 30-day storage period at both 4 °C and 20 °C, suggesting that the presence of clementine pomace imparted antioxidant protection. These findings underscore the efficacy of freeze-dried and homogenized clementine pomace as effective structuring agents for emulsion gels, providing a viable strategy for replacing plastic fat in bakery, pastry, and spreadable food products.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"167 ","pages":"Article 111471"},"PeriodicalIF":11.0,"publicationDate":"2025-04-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143868021","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":"Bio-based emulsifiers through enzymatic hydrolysis of a soy protein isolate","authors":"Giorgia Ballabio ,&nbsp;Letizia Scarabattoli ,&nbsp;Martina Rozzoni ,&nbsp;Marco Aldo Ortenzi ,&nbsp;Giovanna Longhi ,&nbsp;Eleonora Pargoletti ,&nbsp;Marco Rabuffetti ,&nbsp;Carlo F. Morelli ,&nbsp;Giovanna Speranza ,&nbsp;Giuseppe Cappelletti","doi":"10.1016/j.foodhyd.2025.111472","DOIUrl":"10.1016/j.foodhyd.2025.111472","url":null,"abstract":"<div><div>Protein-based surfactants are gaining interest in several industrial sectors, due to their low-cost and biodegradability. Their properties make them a valid bio-based alternative to petrochemical-based tensides, thus reducing environmental and health concerns. To enhance their techno-functional properties, protein structure must be modified. Compared to chemical methods, enzymatic hydrolysis offers an industrially viable and sustainable approach for this purpose. Particularly, by adjusting enzymatic hydrolysis parameters (type of enzyme, incubation time, temperature and pH), the surfactancy of proteins can be substantially altered, broadening both the application range and the conventional emulsifiers choice. In this study, a commercial soy protein isolate (SPI) was hydrolysed through a biocatalytic approach, using Alcalase® 2.4L FG and Protamex® as enzymatic preparations, at different incubation time (15, 120, 360 min). The resulting Soy Protein Hydrolysates (SPHs) were characterised by ultrafiltration with molecular weight cut-off membranes of 10, 5, and 1 kDa. Then, the emulsifying properties of the prepared SPHs were investigated by interfacial tension (IFT) studies. The two hydrolysates, that achieved the greatest IFT reduction, were tested as emulsifiers in simple peanut oil-in-water (O/W) emulsions, prepared with a sonicator device. Their stability over time was evaluated by turbidimetry, emulsion stability index, confocal microscopy images and dynamic light scattering analyses. Protein secondary structures/emulsifying capability relationship was proposed based on circular dichroism (CD) analyses. Furthermore, for potential industrial applications, more complex O/W emulsions (including rheological modifier, solubilizing agent, antioxidants, and buffers) were also formulated using a rotor-stator. Finally, the stability and rheological behavior of these complex emulsions were thoroughly examined.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"167 ","pages":"Article 111472"},"PeriodicalIF":11.0,"publicationDate":"2025-04-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143873226","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":"Ferritin-alginate oligosaccharide shell core complex for co-encapsulation and synergistic stabilization of astaxanthin and zinc ions","authors":"Rui Yang ,&nbsp;Jincan Wu ,&nbsp;Zexu Li ,&nbsp;Yue Li ,&nbsp;Chunkai Gu ,&nbsp;Xinmei Sha ,&nbsp;Li Liang ,&nbsp;Shihao Sun ,&nbsp;Lei Shi ,&nbsp;Yuyu Zhang","doi":"10.1016/j.foodhyd.2025.111470","DOIUrl":"10.1016/j.foodhyd.2025.111470","url":null,"abstract":"<div><div>Ferritin is a natural cage-like protein with multiple interfaces that can be used for encapsulation delivery of bioactive substances. With the increasing demand for nutrients containing multiple bioactive substances, it is important to study the co-encapsulation of bioactive substances with different properties using ferritin as a carrier. In this study, two different bioactive substances, hydrophobic astaxanthin (AST) and mineral Zn²⁺ ions, were encapsulated in the ferritin cavity to fabricate the ferritin-AST-Zn²⁺ complex, and the alginate oligosaccharides (AOS) were further bound to the ferritin to form a ferritin-AST-Zn²⁺-AOS complex. Results showed that each ferritin could load (30.02 ± 1.22) AST and (64.62 ± 0.38) Zn²⁺ ions, and AST could form a complex with Zn²⁺ ions in the ferritin cage. The AST in ferritin-AST-Zn²⁺ complex showed higher thermal, light, and iron ion stabilities and the Zn²⁺ ions in ferritin-AST-Zn²⁺ complex had higher pH and thermal stabilities, showing a synergistic stabilization effect between AST and Zn²⁺ ions. This effect improved the antioxidant properties of ferritin-AST-Zn²⁺ complex. In addition, the binding of AOS on the ferritin facilitated the stability of AST and Zn²⁺ ions. Moreover, the <em>in vitro</em> simulated digestion exhibited that the ferritin-AST-Zn²⁺-AOS complex could sustain the release of AST and Zn²⁺ ions compared with ferritin-AST and ferritin-Zn²⁺ complex, respectively. Ferritin cage is applied as a shell core architecture to deliver bioactive substances with different properties, providing a feasible scheme for ferritin to synergistically stabilize bioactive substances.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"168 ","pages":"Article 111470"},"PeriodicalIF":11.0,"publicationDate":"2025-04-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143882551","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-water interfacial and emulsifying properties of lupin protein and lupin protein-pectin mixtures at neutral and acidic pH conditions","authors":"Xingfa Ma,&nbsp;Mehdi Habibi,&nbsp;Leonard M.C. Sagis","doi":"10.1016/j.foodhyd.2025.111467","DOIUrl":"10.1016/j.foodhyd.2025.111467","url":null,"abstract":"<div><div>Lupin proteins have high nutritional value and can be used to form foams, emulsions, and gels. However, their functionality becomes poor at acidic pH due to reduced protein solubility. Protein solubility and functionality at acidic pH can be improved by adding polysaccharides. In this study, we compared the oil-water interfacial and emulsifying properties of lupin protein isolates (LPI) and LPI-pectin mixtures at pH 7.0, pH 6.0, pH 4.0, and pH 3.5. Overall, LPI-pectin complexes at pH 4.0 and 3.5 showed better interfacial properties and emulsion stabilization than LPI at pH 4.0 and 3.5, while LPI-pectin mixtures at pH 7.0 and 6.0 displayed comparable interfacial and emulsion properties as LPI at 7.0 and 6.0. We observed that LPI at pH 4.0 and pH 3.5 adsorbed faster to the oil-water interface than LPI-pectin complexes at pH 4.0 and 3.5, due to smaller particle sizes of LPI, while LPI and LPI-pectin mixtures at pH 7.0 and 6.0 showed comparable adsorption rates to the oil-water interface. The LPI-pectin mixtures at pH 6.0 and 7.0 formed weak oil-water interfaces, with a stiffness comparable to LPI at these pH values. While at pH 3.5 and 4.0 LPI-pectin complexes formed stiffer oil-water interfaces than LPI. As a result, LPI-pectin complexes at pH 4.0 and 3.5 showed better emulsifying properties and emulsion stability against coalescence during high-shear mixing. The emulsion stabilized with LPI-pectin complex at pH 3.5 showed more extensive flocculation than the complex at pH 4.0, due to the reduced charges of the complex at pH 3.5 and depletion flocculation induced by non-adsorbed complexes. Our study reveals that the complexation of proteins with pectin at acidic pH could be a useful way to improve the oil-water interfacial and emulsifying properties of proteins at acidic pH, and could potentially be used in the food industry to develop plant protein-based emulsion products.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"167 ","pages":"Article 111467"},"PeriodicalIF":11.0,"publicationDate":"2025-04-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143858794","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":"Investigating the dynamics of freeze-drying and annealing using in-situ synchrotron X-ray microtomography","authors":"Shuai Bai Palmkron ,&nbsp;Jonas Engqvist ,&nbsp;Hans Bolinsson ,&nbsp;Björn Bergenståhl ,&nbsp;Stephen Hall ,&nbsp;Samuel McDonald ,&nbsp;Marie Wahlgren ,&nbsp;Emanuel Larsson ,&nbsp;Anna Millqvist Fureby","doi":"10.1016/j.foodhyd.2025.111465","DOIUrl":"10.1016/j.foodhyd.2025.111465","url":null,"abstract":"","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"168 ","pages":"Article 111465"},"PeriodicalIF":11.0,"publicationDate":"2025-04-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143912545","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":"Gelation of tamarind seed polysaccharide induced by tea polyphenols: Screening, gelling kinetics, and properties","authors":"Si Xie ,&nbsp;Huaitian Cui ,&nbsp;Fan Xie ,&nbsp;Zibo Song ,&nbsp;Hui Zhang ,&nbsp;Lianzhong Ai","doi":"10.1016/j.foodhyd.2025.111464","DOIUrl":"10.1016/j.foodhyd.2025.111464","url":null,"abstract":"<div><div>The gelling kinetics and properties of different tea polyphenol-induced gelation of TSP were investigated by rheological and texture techniques. Results showed that epigallocatechin gallate (EGCG), epigallocatechin (EGC), epicatechin gallate (ECG), and gallic acid (GA) were the key factors of tea polyphenols to induce gelation of TSP at different concentration ranges. Sol-gel transition temperatures were determined as 28.8, 15.7, 26.2, and 22.9 °C for TSP/EGCG, TSP/EGC, TSP/ECG, and TSP/GA, respectively from temperature ramp during cooling process. Structure developing rate (SDR) analysis indicated that TSP/EGCG possessed the highest SDR to form gel structure. Non-isothermal kinetic studies demonstrated that all samples needed to overcome high energy barrier at the initial gelling preparation stage during cooling, but much lower <em>Ea</em> at the gel strengthening stage. Besides, a gel aging stage was designated to TSP/EGCG system from 17.72 to 4.00 °C with the lowest <em>Ea</em> (70.16 kJ/mol). These results revealed that gallate and galloyl moieties were the critical structure features of tea polyphenols to promote gelation of TSP, and EGCG showed the strongest ability. Texture tests further found that low temperature and acidic pH were favorable to enhance the mechanical strength of TSP/EGCG gel, but alkaline environment and high content of sucrose weakened the gel structure. This study illustrated the key factors and gelling properties of tea polyphenol-induced gelation of TSP, laying a theoretical foundation to explore polyphenol-response hydrogels in food and biomedicine fields.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"167 ","pages":"Article 111464"},"PeriodicalIF":11.0,"publicationDate":"2025-04-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143851887","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":"Reversible and irreversible changes in protein secondary structure in the heat- and shear-induced texturization of native pea protein isolate","authors":"Hiroshi Nakagawa ,&nbsp;Job Ubbink","doi":"10.1016/j.foodhyd.2025.111453","DOIUrl":"10.1016/j.foodhyd.2025.111453","url":null,"abstract":"<div><div>The molecular mechanism of plant protein texturization under extrusion conditions was unraveled at the secondary structure level by decoupling the effects of heating, cooling and shearing on protein secondary structure. Native pea protein isolate hydrated at 50 % w/w in H₂O and in D₂O, to allow detailed resolution of protein secondary structure, was subjected to temperature cycling in a temperature-controlled ATR-FTIR and was texturized at the gram scale by microcompounding. Upon heating without shearing, native α-helices and intramolecular-β-sheets unfold to random domains, followed by the formation of intermolecular β-sheets, inducing aggregation. During cooling, the intermolecular β-sheets become increasingly ordered, and random domains partially fold into non-native β-structures. Combined heating and shearing results in more extensive β-sheets than heating alone. The resulting β-rich structures provide for an entangled network of protein chains and a cohesive protein matrix. The effect of shear on protein association/dissociation is controlled by the specific mechanical energy (SME), with the degree of intermolecular β-sheet formation increasing with increasing SME values up to ∼1000 kJ/kg, followed by a gradual decrease with further increases of the SME. The detailed molecular insights in the mechanism of plant protein texturization allows for a more controlled design of novel food products, including matrices for use in meat analogues.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"168 ","pages":"Article 111453"},"PeriodicalIF":11.0,"publicationDate":"2025-04-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143874907","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}