Inhibition Mechanism of <i>Pleurotus citrinipileatus</i> Sing. Ergothioneine on Pancreatic Lipase Activity

XIA Zhangchen; MENG Xiaohui; FANG Ru; MAO Yanqing; CHENG Junwen; WANG Yanbin; XU Juan; HE Liang

doi:10.13386/j.issn1002-0306.2024030119

Volume 46 Issue 4

Feb. 2025

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Science and Technology of Food Industry > 2025 > 46(4): 80-89. > DOI: 10.13386/j.issn1002-0306.2024030119

XIA Zhangchen, MENG Xiaohui, FANG Ru, et al. Inhibition Mechanism of Pleurotus citrinipileatus Sing. Ergothioneine on Pancreatic Lipase Activity[J]. Science and Technology of Food Industry, 2025, 46(4): 80−89. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2024030119.

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Inhibition Mechanism of Pleurotus citrinipileatus Sing. Ergothioneine on Pancreatic Lipase Activity

1.
Zhejiang Provincial Key Laboratory of Resources Protection and Innovation of Traditional Chinese Medicine,Zhejiang A&F University, Hangzhou 311300, China
2.
Zhejiang Provincial Key Laboratory of Biological and Chemical Utilization of Forestry Resources,Zhejiang Academy of Forestry, Hangzhou 310023, China
3.
Hangzhou Johncan Mushroom Bio-technology Co., Ltd., Hangzhou 310000, China

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Received Date: March 07, 2024
Available Online: December 07, 2024

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Abstract

Abstract

The interaction between Pleurotus citrinipileatus Sing. ergothioneine (PCEGT) and pancreatic lipase (PL) was studied by analyzing multiple spectroscopies including enzyme kinetics, ultraviolet absorption (UV), fluorescence spectroscopy, synchronous fluorescence spectroscopy and 3D fluorescence spectroscopy as well as the PCEGR-PL interaction mechanism by molecular docking in order to clarify its inhibitory mechanism. The results showed that the inhibition process of PCEGT on PL was reversible non-competitive with 15.29 mg/mL of the half-maximal inhibitory concentration (IC₅₀). The UV spectrum indicated there was a π→π^* transition produced by the peptide bond C=O group of PL as the mass concentration of PCEGT increased, which could reflect the reinforcement of polarity and hydrophilicity. Fluorescence spectra data revealed PCEGT could efficiently static-quench the intrinsic fluorescence of PL by changing its space structure. Based on the Lineweaver-Burk equation, the binding constants (K_a) under three different temperatures were obtained. Among them the K_a value was estimated to be 1.55×10³ L/mol with approximately 1 binding site at 298 K. The thermodynamic parameters including enthalpy change and enthopy change calculated by Van't Hoff's law were to be −8.57 kJ/mol and 2.55 J/(mol·K), respectively. PCEGT might combine with the amino acid residues of PL via hydrogen bonding and electrostatic force. With the increase of the concentration of PCEGT, synchronous fluorescence intensity and 3D fluorescence spectra demonstrated that the failing hydrophobicity and incremental polarity of PL could be achieved evidencing by obvious redshifts of maximum absorption peaks (6 and 3 nm) and descent fluorescence intensities (32.2% and 25.6%). Molecular docking results further reinforced that PCEGT interacted with amino acids outside catalytic site of PL via hydrogen bonding, charge attraction and van der waals' force, resulting in the inhibition of PL. This study was beneficial for the deep understanding the hyperlipidemia of PCEGT from molecular mechanism and boosted the future health food processing of Pleurotus citrinipileatus Sing..
- Pleurotus citrinipileatus Sing.,
- ergothioneine,
- pancreatic lipase,
- inhibitory effect,
- molecular docking

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