Zhou Xu
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Research Interests
Zhou Xu has a total of 151 co-authors. Here are the top co-authors by number of shared publications:
- Mao-Long Chen
School of Food science and Bioengineering, Changsha University of Science & Technology, Changsha 410114, China
23 shared publications Yunhui Cheng
School of Food Science and Bioengineering, Hunan Provincial Key Laboratory of Cytochemistry, Changsha University of Science & Technology, Changsha, 410114, Hunan, China
21 shared publicationsLi Yao
15 shared publicationsKeyu Xing
11 shared publicationsPei Jia
11 shared publications- Yun-Hui Cheng
College of Chemistry and Food Engineering, Changsha University of Science & Technology, Changsha 410114, China
10 shared publications
Latest Publications
- 22 October 2026
- Published by Elsevier in Analytica Chimica Acta
- Vol. 1428
A highly stable T1-MRS sensor based on paramagnetic Gd-MOF for sensitive determination of Cd2+
- 22 October 2026
- Published by Elsevier in Analytica Chimica Acta
- Vol. 1428
A highly stable T1-MRS sensor based on paramagnetic Gd-MOF for sensitive determination of Cd2+
- 19 October 2026
- Published by Royal Society of Chemistry (RSC) in New Journal of Chemistry
- Vol. 50 (40) , 17588-17594
Cooperative Brønsted and Lewis acid sites on Zr-MOF artificial lipase for synthesis of structured lipids
The Brønsted and Lewis acid sites on a Zr-MOF artificial lipase synergistically catalyze the synthesis of structured lipids.
- 19 October 2026
- Published by Royal Society of Chemistry (RSC) in New Journal of Chemistry
- Vol. 50 (40) , 17588-17594
Cooperative Brønsted and Lewis acid sites on Zr-MOF artificial lipase for synthesis of structured lipids
The Brønsted and Lewis acid sites on a Zr-MOF artificial lipase synergistically catalyze the synthesis of structured lipids.
- 27 May 2026
- Published by Elsevier in Food Research International
- Vol. 239, 119556
Bioinspired artificial lipase with engineered hydrophilic microenvironment for oriented substrate binding and structured lipids preparation
- 27 May 2026
- Published by Elsevier in Food Research International
- Vol. 239, 119556
Bioinspired artificial lipase with engineered hydrophilic microenvironment for oriented substrate binding and structured lipids preparation
- Open Access
- 24 February 2026
- Published by Elsevier in SSRN Electronic Journal
Transglutaminase-induced crosslinking of Soy Protein Isolate in Crowded Environments: Effects of Glucan Concentration and Molecular Weight
Dextran with different molecule weights was used as a crowding reagent, and effects of varying degrees of crowding on the TGase-induced crosslinking of SPI were investigated. Results show that the conformations of SPI and TGase tend to become more compact as the crowdedness increases. Low concentrations of DE do not significantly affect the TGase crosslinking of SPI, whereas a highly crowded environment makes TGase unable to effectively crosslink SPI subunits, leading to decreased formation of isopeptide bonds (up to 65.6% decrease compared to the control). Rheological and microstructural properties reveal that increasing the concentration and molecular weight of DE significantly decreases the G' of SPI gels and promotes the formation of inhomogeneous and loose networks. Compared with continuous stirring, intermittent stirring was more conducive to SPI crosslinking and gel formation in a crowded environment, reaching a maximum G' of 603 Pa with a 143.5% increase compared to the unstirred sample.
- 24 February 2026
- Published by Elsevier in SSRN Electronic Journal
Open AccessTransglutaminase-induced crosslinking of Soy Protein Isolate in Crowded Environments: Effects of Glucan Concentration and Molecular Weight
Dextran with different molecule weights was used as a crowding reagent, and effects of varying degrees of crowding on the TGase-induced crosslinking of SPI were investigated. Results show that the conformations of SPI and TGase tend to become more compact as the crowdedness increases. Low concentrations of DE do not significantly affect the TGase crosslinking of SPI, whereas a highly crowded environment makes TGase unable to effectively crosslink SPI subunits, leading to decreased formation of isopeptide bonds (up to 65.6% decrease compared to the control). Rheological and microstructural properties reveal that increasing the concentration and molecular weight of DE significantly decreases the G' of SPI gels and promotes the formation of inhomogeneous and loose networks. Compared with continuous stirring, intermittent stirring was more conducive to SPI crosslinking and gel formation in a crowded environment, reaching a maximum G' of 603 Pa with a 143.5% increase compared to the unstirred sample.
- 9 July 2025
- Published by American Chemical Society (ACS) in Journal of Agricultural and Food Chemistry
- Vol. 73 (33) , 20547-20562
An Overview of Industrial Enzyme Engineering to Achieve a pH Adaptability-Activity Trade-Off: Current Status and Future Perspectives
Enzyme preparations are highly valued in various industries due to their specificity and eco-friendliness. However, natural enzymes often face challenges in extreme pH conditions due to their narrow optimal pH ranges. This limitation highlights the need for enzyme modification that can expand their pH adaptability, enhance stability and activity across varying pH levels, and ultimately increase their industrial utility. To address these challenges, recent advancements in protein engineering have equipped scientists with powerful tools to tailor enzymatic properties. Techniques such as rational design, directed evolution, and computational biology now allow for the precise manipulation of enzyme structures and their functional dynamics. These strategies aim to bridge the inherent limitations of natural enzymes with the stringent requirements of industrial processes, especially in environments in which pH levels can fluctuate significantly. This article focuses on the field of protein engineering and provides a comprehensive review of the latest advancements in modification strategies for acid-tolerant and alkali-tolerant enzymes. It covers a variety of aspects including sequence-guided bioinformatics analysis, structural modifications, regulation of the endogenous force microenvironment, and surface engineering. This study aims to offer diverse perspectives and technical support to help enzymes adapt to the complex and ever-changing landscape of industrial applications.
- 9 July 2025
- Published by American Chemical Society (ACS) in Journal of Agricultural and Food Chemistry
- Vol. 73 (33) , 20547-20562
An Overview of Industrial Enzyme Engineering to Achieve a pH Adaptability-Activity Trade-Off: Current Status and Future Perspectives
Enzyme preparations are highly valued in various industries due to their specificity and eco-friendliness. However, natural enzymes often face challenges in extreme pH conditions due to their narrow optimal pH ranges. This limitation highlights the need for enzyme modification that can expand their pH adaptability, enhance stability and activity across varying pH levels, and ultimately increase their industrial utility. To address these challenges, recent advancements in protein engineering have equipped scientists with powerful tools to tailor enzymatic properties. Techniques such as rational design, directed evolution, and computational biology now allow for the precise manipulation of enzyme structures and their functional dynamics. These strategies aim to bridge the inherent limitations of natural enzymes with the stringent requirements of industrial processes, especially in environments in which pH levels can fluctuate significantly. This article focuses on the field of protein engineering and provides a comprehensive review of the latest advancements in modification strategies for acid-tolerant and alkali-tolerant enzymes. It covers a variety of aspects including sequence-guided bioinformatics analysis, structural modifications, regulation of the endogenous force microenvironment, and surface engineering. This study aims to offer diverse perspectives and technical support to help enzymes adapt to the complex and ever-changing landscape of industrial applications.
- Open Access
Exploring the Potential of an Industry-Scale Microfluidizer for Modifying Rice Starch: Multi-Layer Structures and Physicochemical Properties
The modification effects of industry-scale microfluidizer (ISM) technology on small-sized rice starch remain unknown. This study systematically evaluated the effects of ISM treatment on the structural characteristics (granular morphology, crystallinity, and short-range order) and physicochemical properties (thermal, pasting, and rheological properties) of rice starch. Scanning electron microscopy (SEM) analysis revealed that ISM treatment induced the aggregation of starch granules, leading to an increase in particle size. Furthermore, ISM treatment resulted in starch damage, as evidenced by an increase in the damaged starch content from 4.25% to 17.99%. X-ray diffraction (XRD) analysis found that the relative crystallinity decreased from 29.01% to 20.74%, and Fourier-transform infrared (FTIR) spectroscopy implied that the absorbance ratio of 1047 cm−1/1022 cm−1 decreased from 0.88 to 0.73, indicating the disorganization of long-range crystalline structure and short-range ordered structure. Differential scanning calorimetry analysis demonstrated that ISM treatment reduced the gelatinization enthalpy of rice starch, with a gelatinization degree reaching 31.39%. Rapid visco analyzer (RVA) measurements indicated that ISM treatment increased the pasting viscosity of rice starch. However, the effect of ISM treatment on the dynamic rheological properties was minimal, with a slight enhancement in the loss modulus, while in-shear structural recovery rheology showed no significant impact on the ability of starch gels to recover their original structure. These results suggested that ISM technology effectively modified rice starch, leading to a disrupted structure, increased viscosity, and preserved gel network structure. This approach offers a novel strategy for the application of industry-scale microfluidizers in the development of rice-based products.
Open AccessExploring the Potential of an Industry-Scale Microfluidizer for Modifying Rice Starch: Multi-Layer Structures and Physicochemical Properties
The modification effects of industry-scale microfluidizer (ISM) technology on small-sized rice starch remain unknown. This study systematically evaluated the effects of ISM treatment on the structural characteristics (granular morphology, crystallinity, and short-range order) and physicochemical properties (thermal, pasting, and rheological properties) of rice starch. Scanning electron microscopy (SEM) analysis revealed that ISM treatment induced the aggregation of starch granules, leading to an increase in particle size. Furthermore, ISM treatment resulted in starch damage, as evidenced by an increase in the damaged starch content from 4.25% to 17.99%. X-ray diffraction (XRD) analysis found that the relative crystallinity decreased from 29.01% to 20.74%, and Fourier-transform infrared (FTIR) spectroscopy implied that the absorbance ratio of 1047 cm−1/1022 cm−1 decreased from 0.88 to 0.73, indicating the disorganization of long-range crystalline structure and short-range ordered structure. Differential scanning calorimetry analysis demonstrated that ISM treatment reduced the gelatinization enthalpy of rice starch, with a gelatinization degree reaching 31.39%. Rapid visco analyzer (RVA) measurements indicated that ISM treatment increased the pasting viscosity of rice starch. However, the effect of ISM treatment on the dynamic rheological properties was minimal, with a slight enhancement in the loss modulus, while in-shear structural recovery rheology showed no significant impact on the ability of starch gels to recover their original structure. These results suggested that ISM technology effectively modified rice starch, leading to a disrupted structure, increased viscosity, and preserved gel network structure. This approach offers a novel strategy for the application of industry-scale microfluidizers in the development of rice-based products.
- Open Access
- 4 June 2025
- Published by MDPI AG in Pharmaceuticals
- Vol. 18 (6) , 842
Antioxidant Peptides Derived from Woody Oil Resources: Mechanisms of Redox Protection and Emerging Therapeutic Opportunities
Antioxidant peptides derived from woody oil resource by-products exhibit strong free radical scavenging abilities and offer potential applications in functional foods, nutraceuticals, and cosmetics. This review summarizes the latest advances in preparation technologies, including enzymatic hydrolysis, microbial fermentation, chemical synthesis, recombinant expression, and molecular imprinting, each with distinct advantages in yield, selectivity, and scalability. The structure–activity relationships of antioxidant peptides are explored with respect to amino acid composition, molecular weight, and 3D conformation, which collectively determine their bioactivity and stability. Additionally, emerging delivery systems—such as nanoliposomes, microencapsulation, and cell-penetrating peptides—are discussed for their role in enhancing peptide stability, absorption, and targeted release. Mechanistic studies reveal that antioxidant peptides from woody oil resources act through network pharmacology, engaging core signaling pathways, including Nrf2/ARE, PI3K/Akt, AMPK, and JAK/STAT, to regulate oxidative stress, mitochondrial health, and inflammation. Preliminary safety data from in vitro, animal, and early clinical studies suggest low toxicity and favorable tolerability. The integration of omics technologies, molecular docking, and bioinformatics is accelerating the mechanism-driven design and functional validation of peptides. In conclusion, antioxidant peptides derived from woody oil resources represent a sustainable, multifunctional, and scalable solution for improving human health and promoting a circular bioeconomy. Future research should focus on structural optimization, delivery enhancement, and clinical validation to facilitate their industrial translation.
- 4 June 2025
- Published by MDPI AG in Pharmaceuticals
- Vol. 18 (6) , 842
Open AccessAntioxidant Peptides Derived from Woody Oil Resources: Mechanisms of Redox Protection and Emerging Therapeutic Opportunities
Antioxidant peptides derived from woody oil resource by-products exhibit strong free radical scavenging abilities and offer potential applications in functional foods, nutraceuticals, and cosmetics. This review summarizes the latest advances in preparation technologies, including enzymatic hydrolysis, microbial fermentation, chemical synthesis, recombinant expression, and molecular imprinting, each with distinct advantages in yield, selectivity, and scalability. The structure–activity relationships of antioxidant peptides are explored with respect to amino acid composition, molecular weight, and 3D conformation, which collectively determine their bioactivity and stability. Additionally, emerging delivery systems—such as nanoliposomes, microencapsulation, and cell-penetrating peptides—are discussed for their role in enhancing peptide stability, absorption, and targeted release. Mechanistic studies reveal that antioxidant peptides from woody oil resources act through network pharmacology, engaging core signaling pathways, including Nrf2/ARE, PI3K/Akt, AMPK, and JAK/STAT, to regulate oxidative stress, mitochondrial health, and inflammation. Preliminary safety data from in vitro, animal, and early clinical studies suggest low toxicity and favorable tolerability. The integration of omics technologies, molecular docking, and bioinformatics is accelerating the mechanism-driven design and functional validation of peptides. In conclusion, antioxidant peptides derived from woody oil resources represent a sustainable, multifunctional, and scalable solution for improving human health and promoting a circular bioeconomy. Future research should focus on structural optimization, delivery enhancement, and clinical validation to facilitate their industrial translation.