Food Biophysics
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2022
·Vol. 18
·期 2
·208-217
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IF 3.34
Ren Cong,Quan Tuo,Li Bin
In this work, the effect of a typical colored ingredient- anthocyanin-rich extract (derived from black soybean seed coat extract, abbreviated as BE) on the gelling and digestive properties of soy protein cold-set gels were investigated. The SEM observation revealed that upon the addition of BE, the size of protein aggregates decreased, and more string-of-beads structures appeared in the gel networks. The texture and rheological results demonstrated that BE significantly improved the hardness and storage modulus (G’) of gels, which were related to the enhancement of hydrophobic interactions and disulfide bonds in the gels. Moreover, BE limited the migration of bound water and free water in the gels as well as the in vitro digestion of gels, despite of the swelling ratio of gels in simulated digestive fluids was increased. These findings provide some useful information for the design and application of soybean gel products enriched with colored ingredients in food industry.
研究领域:
食品科学
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生物化学
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DOI
高影响因子
LWT-FOOD SCIENCE AND TECHNOLOGY
·
2023
·
IF 6
Ziyun Liu,Jianming Wang,Chen Yang,Zhuo Wang
Binary gels with various microstructures, including apricot kernel protein isolate-gellan gum gels with high freeze-thaw stability, were obtained by combining transglutaminase covalent cross-linking and gellan gum modification. Adding 0–0.1% gellan gum (w/w) can form continuous protein network structures dominated by covalent networks and disulfide bonds. In addition to covalent cross-linking, the increase in the strength of hydrophobic and electrostatic interactions at gellan gum concentrations below 0.2% (w/w) facilitated the formation of a bicontinuous network (AGG3). When excess gellan gum was added (0.03%, w/w), gellan gelation occurred in the system, leading to the formation of heterogeneous aggregated structures (AGG4). Confocal laser microscopy revealed a dense porous structure in the continuous protein network after freeze-thaw treatment, and AGG4 showed heterogeneous and loose aggregated microstructure, while the bicontinuous network structure was maintained. The water holding capacity of AGG3 was increased by 21.36% after freezing compared with the gels without gellan gum, and AGG3 maintained high hardness and springiness. Low-field nuclear magnetic resonance and magnetic resonance imaging showed that the bicontinuous network was more conducive to the tethering ability and uniform distribution of hydrogen protons than the continuous network structure of proteins. Therefore, AGG3 exhibited excellent freeze-thaw stability.
研究领域:
食品科学
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生物化学
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DOI
高影响因子
FOOD RESEARCH INTERNATIONAL
·
2024
·
IF 7
Yanfei Xu,Zheng Zhou
While heat treatment is a conventional method for the gelation of alkaline-extracted walnut protein isolates (AWPI), it can limit the incorporation of heat-sensitive ingredients. This study explored a novel approach to fabricate cold-set gels from epigallocatechin-3-gallate (EGCG) conjugated AWPI (AWPI-EGCG). EGCG conjugation effectively inhibited the thermal gelation of AWPI while promoting the formation of soluble aggregates upon heat treatment. AWPI-EGCG cold-set gels were then successfully fabricated through acidification with glucono-δ-lactone (GDL). The rheological study revealed that the storage modulus and yield stress of the cold-set gels were positively correlated with the GDL concentration and the EGCG conjugation degree. However, higher concentrations of GDL were associated with the reduced yield strain of the gels. Texture analysis indicated an increase in gel hardness with increasing GDL concentration, accompanied by a decrease in springiness. Microstructural examination by scanning electron microscopy revealed that the AWPI-EGCG cold-set gels with 0.3 % GDL exhibited smaller pores with thinner and smoother internal walls, while those with 0.9 % GDL exhibited relatively larger pores with thicker and denser walls. In addition, the AWPI-EGCG cold-set gels showed promising quercetin encapsulation capacities and controlled release properties.
研究领域:
食品科学
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生物技术
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材料科学
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产品关联
DOI
PubMed
高影响因子
FOOD HYDROCOLLOIDS
·
2023
·
IF 10.7
Qiaoyan Wang,Changyu Zhou,Qiang Xia,Daodong Pan,Lihui Du,Jun He,Yangying Sun,Fang Geng,Jinxuan Cao
In order to investigate the effect of pH treatments on the coacervation mechanism of fibrinogen hydrolysates and carrageenan complex, the cold-set hydrogels of carrageenan and fibrinogen hydrolysates derived from the hydrolysis of chymotrypsin, alcalase and flavourzyme were prepared under different pH; mechanical strength, rheological properties, gelling structure, morphological observation, and chemical action force were investigated, and the antioxidant capacity of the hydrogels was further evaluated in meat preservation model. The results indicated that the hydrogels of carrageenan and fibrinogen hydrolysates derived from the hydrolysis of alcalase (AHs) showed the largest gel strength and the best viscoelasticity at pH 7.0 compared with other pH and hydrolase treatments. FTIR spectrum revealed that AHs showed more β-sheet and β-turn at pH 7.0 among all treatments. The interaction forces of these hydrogels showed various under different pH and hydrolase treatments, and the network of AHs hydrogels at pH 7.0 was mainly stabilized by electrostatic interaction and hydrophobic interaction. SEM and AFM demonstrated that the more regular three-dimensional network with smaller pore sizes was formed in AHs at pH 7.0 compared with pH 5.0 and pH 9.0. The AHs showed the largest scavenging ability for DPPH radicals (72.4%) at pH 7.0 in vitro , and the coated meat samples with AHs significantly increased the preservation times of fresh pork and dry-cured ham during the storage by inhibiting the increase of TBARS, TVB-N, and metmyoglobin. The finding of this work is expected to broaden the application of fibrinogen hydrolysate hydrogels into the field of food industry.
研究领域:
食品科学
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材料科学
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生物技术
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DOI
高影响因子
Food Bioscience
·
2022
·
IF 5.318
Jiang-lan Yuan,Chang-sheng Ding,Cheng-liang Li,Yu Zhang,Xu Kang
Protection and embedding of hydrophobic bioactive compounds using protein hydrogels are emerging focus during the latest decade. In present study, we fabricated the porcine plasma protein (PPP) cold-set gel by microbial transglutaminase (MTGase) and glucono-δ-lactone (GDL) as coupling precursors. As a result, the embedding, protection and controlled-release effect of the gel on vulnerable hydrophobic bioactive components (quercetin (Que) as representative) with proposed molecular mechanisms were investigated in detail. The results showed that high concentration of Que (5 mmol/L) could be loaded with PPP cold-set gel and embedding efficiency (EE) was over 98%. Compared with free Que, the embedded one exhibited significantly higher thermostability , photochemical stability and storage stability ( P < 0.05). In addition, the gel loaded with 5 mmol L −1 of Que had higher swelling potency under gastric (low pH) media and controlled release performance following simulated intestinal digestive pathway. Water holding capacity (WHC) implied that free water molecules played less role in the retention ability of Que in fabricated gel network. Spectral-assisted structural characterization proved that Que was efficiently embedded mainly by generating PPP-Que complex through hydrogen bond and van der Waals force, and the binding site was mainly near Trp residue. This work gave novel insight into the potential use of PPP cold-set gel as an excellent carrier towards protection and selective delivery of vulnerable small hydrophobic nutraceutical compounds.
研究领域:
食品科学
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生物技术
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营养保健品
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蛋白质化学
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产品关联
DOI
高影响因子
FOOD HYDROCOLLOIDS
·
2024
·
IF 11
Qi Qi,Xiaopian Yan,Yuxuan Mao,Fang Wang,Hao Zhang,Xiuying Xu,Yuzhu Wu,Chengbin Zhao,Jingsheng Liu
Soybean protein isolate (SPI) and red bean protein isolate (RBPI) were mixed with common starch (CS) and waxy starch (WS) from corn respectively, and then subjected to glucono-δ-lactone (GDL)-induced crosslinking to form the protein–starch complex cold gels, which was used as a delivery carrier for curcumin. The complex gel with addition of CS had denser network structure and higher gel strength, resistance to deformation and viscoelasticity, while the complex gel with WS had the opposite effect. The protein interacted more strongly with CS than WS, enhancing the structural and thermal stability of the complex gel, which resulted in a higher curcumin encapsulation ratio in the gel and its chemical stability during light and heat treatment. The intensity and location of many characteristic absorption peaks in the infrared spectra changed during simulated gastrointestinal digestion, which indicated the destruction of gel structure, leading to the transformation of α-helix and β-sheet into β-turn and random coil in the secondary structure. The addition of CS and WS reduced the release of curcumin in gastric phase, but promoted its directional release in intestinal phase, due to the changes in the digestion pattern of the complex gel, especially the complex gel with addition of WS had a better controlled release effect, which was also related to the more disordered and flexible secondary structure of its gastric digests. The protection of curcumin by gel network and the targeted release behavior of curcumin during intestinal digestion improved its bioaccessibility. In addition, the curcumin in RBPI-based gels had higher encapsulation ratio, chemical stability and bioaccessibility than that in SPI-based gels. Therefore, protein–starch complex cold gels can be used as controlled release carriers for the protection and delivery of sensitive bioactive compounds or nutrients.
研究领域:
食品科学
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生物技术
·
药学
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材料科学
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产品关联
DOI
高影响因子
Food Chemistry-X
·
2023
·
IF 6.1
Chengbin Zhao,Zhenchi Miao,Qi Qi,Qihang Zheng,Yuxuan Mao,Zejun Chu,Hao Zhang,Xiuying Xu,Mingzhu Zheng,Jingsheng Liu
Soy protein isolate (SPI) was mixed with different concentrations of common starch (CS) and waxy starch (WS) from corn. The interactions of SPI with CS or WS and their effects on the acid-induced cold gelation properties of complexes were investigated. Compared with WS, SPI could bind to CS more strongly and formed a tighter SPI–CS non-covalent complex, which resulted in the increased β-sheet and a more ordered secondary structure. The gel strength, water holding capacity (WHC), viscoelasticity, hydrophobic interactions and thermal stability of SPI–CS complex gels were enhanced as increasing CS concentration, and the complex with 2% of CS had the best gelation properties. Although adding WS reduced the gel strength, rheological properties and hydrophobic interactions of SPI–WS complex gels, it improved the WHC and thermal stability of the complex gels. Therefore, CS had a broader effect on improving acid-induced cold gelation properties of SPI than WS.
研究领域:
食品科学
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化学
·
生物物理学
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产品关联
DOI
PubMed
高影响因子
JOURNAL OF FOOD ENGINEERING
·
2016
·
IF 3.199
Bohui Liu,Hui Wang,Tan Hu,Peipei Zhang,Zhuo Zhang,Siyi Pan,Hao Hu
In this study, the effect of ball-milling (BM, Mixer Mill MM 400) treatments on the physicochemical properties of soybean protein isolate (SPI) and its cold-set gels induced by glucono-δ-lactone was studied. BM of SPI increased the gel strength and water holding capacity of cold-set gels significantly after 4 min of BM treatments. BM treatments did not alter the primary structure of SPI, but caused minor changes of the secondary structure. Furthermore, surface hydrophobicity of SPI increased gradually from 2058 to 5051 after 10 min of BM, while free SH groups reduced from 3.92 to 2.65 μmol/g protein. Moreover, near-UV CD spectra indicated that the tertiary conformation stability was increased and the hydrophobic groups might shift to a more hydrophobic microenvironment. In conclusion, appropriate BM treatments could change the physicochemical properties of SPI and increased the gelation properties of SPI cold-set gels.
研究领域:
食品科学
·
蛋白质化学
·
材料科学
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产品关联
DOI
高影响因子
FOOD CHEMISTRY
·
2022
·
IF 9.231
Xinsheng Qin,Qingli Bo,Panzhu Qin,Sufang Wang,Kaiyong Liu
In this study, we demonstrated the role of whey protein isolate (WPI)/(−)-epigallocatechin-3-gallate (EGCG) covalent conjugates/gellan gum double network emulsion gels by duo-induction of glucono-δ-lactone (GDL) and CaCl 2 on the digestion viability of Lactobacillus Plantarum powders. We employed a novel one-step continuous cold gelation strategy to product double network emulsion gels. The gellan gum in continuous phase was first induced by CaCl 2 to form a gel in a short time. Besides, the GDL was improved covalent cross-linking between WPI-EGCG covalent conjugate Pickering particles or particle-coated oil droplets because of the slowly pH reduction. The first cross-linked gellan gum gels could be more closely integrated into the GDL-induced second gel networks with synergistic role, which promoted the formation of compact and homogeneous networks through hydrophobic interactions and disulfide bonds. Thus, the results provide a promising strategy for probiotic powders encapsulation of double network emulsion gels in oral applications of gel type foods.
研究领域:
食品科学
·
生物技术
·
药学
·
材料科学
✓ 已验证
产品关联
DOI
PubMed
高影响因子