FOOD CHEMISTRY
·
2020
·
IF 6.306
Xin Chen,Zhiwen Guo,Junjie Zhang,Yingying Li,Rui Duan
The denaturation temperature of collagen has been determined using several methods, such as circular dichroism, fourier transform infrared spectroscopy, and differential scanning calorimetry, etc. Such methods need specific equipment or mass samples (more than 75 mg samples), which means higher inspection costs. In this study, Sirius red was employed to determine the Tds of collagen from calf tendon, silver carp skin, frog and salmon skins (38.2 °C, 32.6 °C, 33.8 °C, and 15.6 °C, respectively) to explore a new method that does not require special equipment and only needs 2–3 mg sample for one measurement. This method was suitable for the determination of the denaturation temperature of collagen from terrestrial, aquatic and amphibian animals. Analysis of variance and t -test revealed that no significant difference was found between Sirius Red and viscosity methods. However, the Sirius Red method needs simpler equipment and less sample than viscosity and other methods. So it could be used as a convenient approach to determine the denaturation temperature of collagen instead of the viscosity method.
研究领域:
生物化学
·
材料科学
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产品关联
DOI
PubMed
高影响因子
LWT-FOOD SCIENCE AND TECHNOLOGY
·
2021
·
IF 4.952
Yidan Zhang,Xuebing Zhang,Zhiheng Zhang,Zhenjia Chen,Xu Jing,Xiaowen Wang
The main purpose of this study was to investigate the effects of HHP pressure on the structure and physicochemical properties of millet gliadin. The effects of HHP pressure on its physicochemical properties, structure, and conformation were systematically studied by ultraviolet second derivative spectroscopy, fluorescence spectroscopy, Fourier transform infrared spectroscopy, and particle size analysis. HHP pressure treatment changed the spatial conformation of millet gliadin and increased the hydrophilicity of gliadin, but it did not alter the distribution of subunits. HHP pressure treatment changed the surface charge distribution of protein and increased the aggregation degree of protein, leading to the increase in protein particle size. After treatment, the α-helices and random coil ratio of the protein decreased, and some disulfide bonds formed, which made the protein structure more orderly and led to an increase in denaturation temperature. This phenomenon helped improve the limitation that millet gliadin cannot be directly used in the field of food production due to its strong hydrophobicity.
研究领域:
食品科学
·
蛋白质化学
·
生物物理学
✓ 已验证
产品关联
DOI
高影响因子
FOOD HYDROCOLLOIDS
·
2025
·
IF 12.4
Si-Jie Wu,Qi-Bin Kuang,Ran Feng,Ran Meng,Qiu-Ya Ji,Han Tao,Bao-Cai Xu,Bao Zhang
Heat treatment, as one of the most common processing methods in protein modification, has unclear mechanisms affecting protein-polyphenol interactions. This study investigated the effects of sub-denaturing temperature pretreatment on protein structure-function relationships and their interactions with polyphenols using the quercetin-lactoferrin (Que-LF, QLF) system as a model. Results demonstrated that among 25-55 °C gradient heat treatments, LF pretreated at 40 °C (LF40) formed metastable aggregates through moderate structural unfolding, with significantly exposed hydrophobic cavities that enhanced binding affinity to Que ( K a =7.11×10 5 L/mol). Preheating optimized the conformational flexibility and spatial compatibility of LF binding pockets, enabling Que to embed into hydrophobic cavities via hydrophobic interactions ( ΔH = 23.82 kJ·mol -1 , ΔS = 188.27 J·mol -1 ·K -1 ) and multiple hydrogen bonding networks. The QLF40 complex exhibited optimal binding free energy (-85.1 kJ/mol) and conformational stability. Furthermore, Que binding synergistically improved thermal stability (2 °C increase in denaturation temperature) and antioxidant activity (64.7% DPPH and 98.4% ABTS scavenging rates) of the complex through masking hydrophobic sites, strengthening hydrogen bond networks, and inducing local structural rigidity. This study provides theoretical foundation for designing efficient active ingredient delivery systems based on controlled protein structural modification.
研究领域:
食品科学
·
生物化学
·
分子生物学
·
生物物理学
·
营养学
✓ 已验证
产品关联
DOI
高影响因子
CHINESE JOURNAL OF CHEMICAL ENGINEERING
·
2024
·
IF 3.7
Liming Zhang,Xinmeng Liu,Haoyue Li,Lei Zhang
Ligament cryopreservation enables a prolonged shelf life of allogeneic ligament grafts, which is fundamentally important to ligament reconstruction. However, conventional cryopreservation techniques fail to eliminate the damage caused by ice crystal growth and the toxicity of cryopreservation agents (CPAs). Here, we report a novel CPA vitrification formulation primarily composed of betaine for ligament cryopreservation. Comprehensive optimization was conducted on the methods for vitrification and rewarming, as well as the loading and unloading conditions, based on the critical cooling rate (CCR), critical warming rate (CWR), and permeation properties of the cryoprotectant. Using biomechanical and histological level tests, we demonstrate the superior performance of our method in ligament cryopreservation. After 30 days of vitrification cryopreservation, parameters such as the Young's modulus, tensile stress, denaturation temperature, and glycosaminoglycans (GAGs) content of the ligament remained essentially unchanged. This work pioneers the application of ice-free cryopreservation for ligament and holds great potential for improving the long-term storage of ligament, providing valuable insights for future technique development.
研究领域:
组织工程
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生物力学
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低温生物学
·
骨科
✓ 已验证
产品关联
DOI
高影响因子
JOURNAL OF CEREAL SCIENCE
·
2023
·
IF 3.8
Min Zhang,Kai Huang,Jun Lu,Anni Lu,Xiao Guan,Yu Zhang,Sen Li,Hongdong Song,Hongwei Cao,Zhu Sun,Zhiquan Yu
The aim of this study was to develop a novel plant-based milk using oat core flour (OCF) as the raw material. OCF was firstly treated with deep liquefaction and saccharification . After that, multienzyme treatments, including protease, lipase , and cellulase hydrolyzations, were optimized and applied. The physicochemical properties of the oat milk were characterized. Particle size distribution and zeta potential determinations showed that neutral protease and lipase could effectively prevent the phase separation of oat milk. The highest absolute zeta potential value and narrower particle distribution were obtained at pH 7. Microstructure analysis showed that neutral protease treatment prevented protein aggregations, whereas the cellulase treatment destroyed the network structures formed by the fibers. Multienzyme treatments decreased the centrifugal sedimentation rate (SR) of OCF and increased the water absorption index (WSI) and the denaturation temperature. Furthermore, multienzyme treatments improved the sensory acceptance of color and apparent viscosity. Above all, this research was of specific significance to the development, application, and industrialization of OCF.
研究领域:
食品科学
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化学工程
·
感官科学
✓ 已验证
产品关联
DOI
高影响因子
INTERNATIONAL JOURNAL OF FOOD PROPERTIES
·
2019
·
IF 1.398
Guang-Long Yao,Wei He,You-Gen Wu,Jian Chen,Xin-Wen Hu,Jing Yu
This study aimed to analyze the effect of hydrogen peroxide decolorization on the structure and functional characteristics of tea meal protein to provide some theoretical basis for the utilization of tea meal protein. The changes in the protein structure and function before and after decolorization were evaluated by measuring denaturation temperature, surface hydrophobicity, and sulfhydryl content and by analyzing infrared spectrum, X-ray diffraction peak, and microstructure, etc. Results showed that decolorization with hydrogen peroxide increased the surface hydrophobicity, decreased the sulfhydryl content, and did not change the disulfide bond content. The treatment weakened the chemical bond strength but did not affect the basic skeleton structure. The microstructure as well as the position and intensity of the X-ray diffraction peak of the protein from Camellia oleracea seed cake remained the same before and after the treatment. The heat denaturation temperature also increased. Hydrogen peroxide did not change the isoelectric point; decreased the solubility, emulsifying properties, emulsion stability, foaming ability, and foam stability of the protein; and increased the oil and water holding capacities. Overall, decolorization with hydrogen peroxide did not significantly affect the protein structure but changed its functional properties.
研究领域:
食品科学
·
蛋白质化学
·
农业生物技术
✓ 已验证
产品关联
DOI
高影响因子
FOOD CHEMISTRY
·
2024
·
IF 8.5
Si-Jie Wu,Ran Feng,Ran Meng,Qiu-Ya Ji,Han Tao,Bao-Cai Xu,Bao Zhang
Denaturation and/or aggregation of proteins under adverse environmental conditions can greatly impair their bioactivity and functional properties. Based on this, this study aims to improve the functional properties of lactoferrin by complexing with berberine and investigate the mechanism using multispectral techniques, molecular docking and dynamics simulations. The results showed that berberine bound to lactoferrin through hydrogen bonding and van der Waals forces and altered its conformation, surface hydrophobicity, amino acid microenvironment, and secondary structure. Molecular docking and dynamics simulations further revealed that berberine inhibited the drastic changes in the lactoferrin structure, contributing to the complex stability. Consequently, the denaturation temperature and degradation temperature (224 °C to 230 °C) and the tolerance to extreme pH, high temperature, and ions of the lactoferrin-berberine complex were improved. This study systematically revealed the mechanism of berberine to improve the functional properties of lactoferrin, contributing to the development and application of novel functional ingredients.
研究领域:
生物化学
·
分子生物学
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药学
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食品科学
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生物物理学
✓ 已验证
产品关联
DOI
PubMed
高影响因子
Innovative Food Science & Emerging Technologies
·
2024
·
IF 6.3
Wujun You,Hongge Liu,Benjamin Ndeshipanda Kashenye,Yinghao Li,Huijuan Zheng,Qiuting Zhang
The research on the application of ultrasound in food processing has been increasing in recent years. In particular, using ice-bath temperature-controlled ultrasound (IBU) to minimize the effects of thermal aspects has been the main focus. However, this approach does not maximize the utilization of energy. Therefore, this study aims to compare the effect of non-temperature-controlled ultrasound (NTU) and temperature-controlled ultrasound (TU), with IBU on the structure and properties of zein. To further explore the role and mechanism of thermal effects in ultrasound processes. Firstly, particle size, zeta potential, hydrophobicity, and thermal stability of zein nanoparticles prepared using various ultrasound-assisted methods were characterized. Compared to the particle size in the IBU group, the NTU group consistently had smaller particles under the same power conditions (e.g., 197 nm versus 176 nm at U1). The particle size in the TU group changes depending on the temperature (e.g., from native 225 nm down to 185 nm). As for the denaturation temperatures, the NTU group (88.9 °C) was significantly higher than that of the IBU (75.76 °C) and TU groups (e.g., 76.9 °C at treatment temperatures of 30 °C). In all, IBU reduces the thermal stability, while NTU treatment enhances it. Furthermore, UV, fluorescence, and CD spectra results indicate that both NTU and TU groups significantly reduce the α-helix structure by unfolding and exposing more internal hydrophobic groups of zein than the IBU group. These results indicate that the effects of ultrasound on zein are closely related to the heating source during the ultrasonic process. IBU could be utilized to maximize the reduction of denaturation levels, but NTU may exhibit superior performance such as protein modification, reducing particle size, or enhancing stability in industrial production.
研究领域:
食品科学
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材料科学
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物理化学
✓ 已验证
DOI
高影响因子
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
·
2021
·
IF 6.953
Yuqing Lei,Sihai Gao,Xiaole Xiang,Xiuting Li,Xiongwei Yu,Shugang Li
Low-sugar and high-protein adhesives have broad market application prospects, while natural plant proteins have confronted technical bottlenecks due to their poor adhesion. In this study, the effects of ethanol with different concentrations (0–80%) on the adhesion properties of walnut protein isolate-xanthan gum (WNPI-XG) composite adhesives were investigated. Results showed the bonding strength of WNPI-XG treated with 40% ethanol reached 12.55 MPa, the denaturation temperature and the surface hydrophobicity increased to 87.91 and 185.07 respectively, displaying the best rheological and texture properties. It also indicated appropriate concentration of ethanol (40%) didn't change the molecular weight of WNPI-XG, but greatly strengthened the fluorescence intensity, leading changes in contents of reactive sulfhydryl groups, electrostatic forces, hydrophobic interactions, hydrogen bonds and disulfide bonds . Furthermore, the treatment also facilitated a conformation conversion of the secondary structures from β -sheet to α-helix, promoting the full unfolding of protein molecules . The microstructure analysis showed after 40% ethanol treatment, the WNPI structure was uniform, the surface of WNPI-XG adhesive was flat and smooth, combined more closely with water molecules. By analyzing the influence of ethanol treatment on adhesion of WNPI-XG, the research laid a theoretical foundation for protein modification, providing good technical references for its development and utilization.
研究领域:
材料科学
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化学工程
·
食品科学
·
生物技术
✓ 已验证
产品关联
DOI
PubMed
高影响因子
RSC Advances
·
2020
·Vol. 10
·期 49
·29555-29566
·
IF 3.119
Hongyin Zhang,Shuai Shao,Rongxin Han,Rongrong Zhang,Xintong Ma,Miao Wang,Zhiqiang Wan,Daqing Zhao,Mingming Yan
Semen Ziziphi Spinosae (Ziziphus jujuba Mill. var. spinosa (Bunge) Hu ex H. F. Chou) is a functional food and a traditional Chinese medicine (TCM) in China. Herein, Semen Ziziphi Spinosae protein (SZSP) was prepared by an alkaline extraction and acid precipitation method, of which the structural, physicochemical, functional and emulsion properties were investigated. Results showed that SZSP contained an ideal amino acid composition. The structural properties of the proteins were characterized using Fourier transform infrared spectroscopy (FTIR), relative fluorescence and circular dichroism (CD) spectroscopy analysis. The electrophoresis profiles showed that the main molecular weight of the protein components was about 10–40 kDa and contained some glycoproteins. Differential scanning calorimetry analysis indicated that the denaturation temperature of SZSP was 110.5 °C. The functional properties showed that SZSP has good water and oil absorption capacity, high emulsifying ability and foaming stability. The overall results suggest that SZSP is a promising protein source for the functional food industry.
研究领域:
食品科学
·
药学
·
生物化学
✓ 已验证
产品关联
DOI
PubMed
高影响因子
ACS Omega
·
2020
·
IF 2.87
Junhui Yang,Cuicui Ding,Lele Tang,Feng Deng,Qili Yang,Hui Wu,Lihui Chen,Yonghao Ni,Liulian Huang,Min Zhang
Because of poor water solubility and low thermostability, the application of collagen is limited seriously in fields such as injectable biomaterials and cosmetics. In order to overcome the two drawbacks simultaneously, a novel bifunctional modifier based on the esterification of polyacrylic acid (PAA) with N-hydroxysuccinimide (NHS) was prepared. The esterification degree of PAA-NHS esters was increased upon increasing the NHS dose, which was confirmed by Fourier-transform infrared (FTIR) and nuclear magnetic resonance spectrascopy. FTIR results indicated that the triple helix of the modified collagens remained integrated, whereas the molecular weight became larger, as reflected by the sodium dodecyl sulfate–polyacrylamide gel electrophoresis pattern. The modified collagens displayed excellent water solubility under neutral condition, owing to lower isoelectric point (3.1–4.3) than that of native collagen (7.1). Meanwhile, denaturation temperatures of the modified collagens were increased by 4.8–5.9 °C after modification. The modified collagen displayed hierarchical microstructures, as reflected by field-emission scanning electron microscopy, while atomic force microscopy further revealed a “fishing net-like” network in the nanoscale, reflecting a unique aggregation behavior of collagen macromolecules after modification. As a whole, the PAA-NHS ester as a bifunctional modifier endowed collagen with desired water solubility and thermostability in a conflict-free manner, which was beneficial to the process and application of the water-soluble collagen.
研究领域:
生物材料
·
化妆品
·
材料科学
·
化学工程
✓ 已验证
产品关联
DOI
PubMed
高影响因子
Marine Drugs
·
2023
·Vol. 21
·期 5
·260
·
IF 5.4
Zhilin Pan,Baolin Ge,Mingjun Wei,Jeevithan Elango,Wenhui Wu
Numerous studies have shown that type II collagen (CII) has a potential role in the treatment of rheumatoid arthritis. However, most of the current studies have used terrestrial animal cartilage as a source of CII extraction, with fewer studies involving marine organisms. Based on this background, collagen (BSCII) was isolated from blue shark (Prionace glauca) cartilage by pepsin hydrolysis and its biochemical properties including protein pattern, total sugar content, microstructure, amino acid composition, spectral characteristics and thermal stability were further investigated in the present study. The SDS-PAGE results confirmed the typical characteristic of CII, comprising three identical α1chains and its dimeric β chain. BSCII had the fibrous microstructure typical of collagen and an amino acid composition represented by high glycine content. BSCII had the typical UV and FTIR spectral characteristics of collagen. Further analysis revealed that BSCII had a high purity, while its secondary structure comprised 26.98% of β-sheet, 35.60% of β-turn, 37.41% of the random coil and no α-helix. CD spectra showed the triple helical structure of BSCII. The total sugar content, denaturation temperature and melting temperature of BSCII were (4.20 ± 0.03)%, 42 °C and 49 °C, respectively. SEM and AFM images confirmed a fibrillar and porous structure of collagen and denser fibrous bundles formed at higher concentrations. Overall, CII was successfully extracted from blue shark cartilage in the present study, and its molecular structure was intact. Therefore, blue shark cartilage could serve as a potential source for CII extraction with applications in biomedicine.Keywords:type II collagen;blue shark (Prionace glauca) cartilage;microstructure;thermal stability
研究领域:
生物化学
·
生物技术
·
海洋生物学
·
医学
✓ 已验证
产品关联
DOI
PubMed
高影响因子
危险品化学品经营许可证（带存储）