收藏切换
Effect of p-Hydroxybenzoic Acid on the Activation of β-Glucosidase Activity and Their Interaction
收藏切换
Shunfeng LI1, Yunli CHEN2, Xueyi LAN2, Luyao FENG2, Anjian WANG1, Xiaoyuan WANG2, 3, Lihua ZHANG2, 3, *
Science and Technology of Food Industry | 2026, 47(4) : 89 - 96
Less
收藏切换
Science and Technology of Food Industry | 2026, 47(4): 89-96
• Research and Investigation •
Effect of p-Hydroxybenzoic Acid on the Activation of β-Glucosidase Activity and Their Interaction
Full
Shunfeng LI1, Yunli CHEN2, Xueyi LAN2, Luyao FENG2, Anjian WANG1, Xiaoyuan WANG2, 3, Lihua ZHANG2, 3, *
Affiliations
  • 1Research Center of Agro-products Processing Science and Technology, Henan Academy of Agricultural Sciences, Zhengzhou 450002, China
  • 2College of Food and Bioengineering, Zhengzhou University of Light Industry, Zhengzhou 450001, China
  • 3Key Laboratory of Cold Chain Food Processing and Safety Control, Ministry of Education, Zhengzhou University of Light Industry, Zhengzhou 450001, China
Published: 2026-02-15 doi: 10.13386/j.issn1002-0306.2025020266
Outline
收藏切换

To investigate the effect of phenolic acids on the activity of β-glucosidase, this study systematically evaluated the activation mechanism of p-hydroxybenzoic acid (PHBA) at varying concentrations (0~0.5 g/L) through circular dichroism spectroscopy and molecular docking, with a focus on enzyme conformational dynamics and molecular interactions. The results showed that PHBA significantly enhanced β-glucosidase activity in a concentration-dependent manner. Secondary structural analysis revealed that the content of α-helix significantly decreased by 52.14% (P<0.05), while β-sheet, β-turn, and random coil structures increased by 90.20%, 27.24%, and 50.56%, respectively, at 0.5 g/L PHBA compared to the control group. These structural shifts suggestted that the enzyme's active site might reside within α-helix regions. Fluorescence quenching assays confirmed spontaneous binding between PHBA and β-glucosidase, with one or one class of binding sites identified. Molecular interaction analyses revealed that hydrogen bonding, van der Waals forces, and hydrophobic interactions predominantly stabilized the PHBA-enzyme complex. Molecular dynamics simulations further validated the structural stability of the PHBA-β-glucosidase complex over 100 ns trajectories (RMSD<0.4 nm), confirming PHBA as a potent β-glucosidase activator. This study elucidates the molecular basis of PHBA-driven enzyme activation and provides a theoretical foundation for enhancing β-glucosidase activity in phenolic acid-rich fermented fruit and vegetable products.

p-hydroxybenzoic acid  /  β-glucosidase  /  circular dichroism  /  fluorescence quenching  /  molecular docking
李顺峰, 陈云莉, 兰雪怡, 冯路瑶, 王安建, 王小媛, 张丽华. 对羟基苯甲酸对β-葡萄糖苷酶的激活效应及其互作关系. 食品工业科技, 2026 , 47 (4) : 89 -96 . DOI: 10.13386/j.issn1002-0306.2025020266
Shunfeng LI, Yunli CHEN, Xueyi LAN, Luyao FENG, Anjian WANG, Xiaoyuan WANG, Lihua ZHANG. Effect of p-Hydroxybenzoic Acid on the Activation of β-Glucosidase Activity and Their Interaction[J]. Science and Technology of Food Industry, 2026 , 47 (4) : 89 -96 . DOI: 10.13386/j.issn1002-0306.2025020266
Year 2026 volume 47 Issue 4
111
48
Cite this Article
BibTeX
Article Info
doi: 10.13386/j.issn1002-0306.2025020266
  • Receive Date:2025-03-03
  • Online Date:2026-10-24
  • Published:2026-02-15
Article Data
Affiliations
History
  • Received:2025-03-03
Affiliations
    1Research Center of Agro-products Processing Science and Technology, Henan Academy of Agricultural Sciences, Zhengzhou 450002, China
    2College of Food and Bioengineering, Zhengzhou University of Light Industry, Zhengzhou 450001, China
    3Key Laboratory of Cold Chain Food Processing and Safety Control, Ministry of Education, Zhengzhou University of Light Industry, Zhengzhou 450001, China
References
Share
https://castjournals.cast.org.cn/joweb/spgykj/EN/10.13386/j.issn1002-0306.2025020266
Share to
QR

Scan QR to access full text

Cite this article
BibTeX
Citations
表12种不同金属材料的力学参数
科
Family
属数
Number of
genus
种数
Number of
species
占总种数比例
Percentage of
total species (%)
属
Genus
种数
Number of
species
占总种数比例
Percentage of total
species (%)
鹅膏菌科Amanitaceae 2 11 5.26 鹅膏菌属 Amanita 10 4.78
小菇科 Mycenaceae 2 12 5.74 丝盖伞属 Inocybe 5 2.39
多孔菌科 Polyporaceae 8 14 6.70 蜡蘑属 Laccaria 5 2.39
红菇科 Russulaceae 3 23 11.00 小皮伞属 Marasmius 6 2.87
小菇属 Mycena 11 5.26
光柄菇属 Pluteus 5 2.39
红菇属 Russula 17 8.13
栓菌属 Trametes 5 2.39
关闭全屏
  • BibTeX
  • EndNote
  • RefWorks
  • TxT