The Thermal Denaturation Conditions of <i>β</i>-galactosidase in <i>Kluyveromyces lactis</i> under Molecular Dynamics Simulation

CAO Kun; WANG Ruonan; XIONG Xingdong; WU Yun; LIU Xinguang

doi:10.6054/j.jscnun.2022028

Journal of South China Normal University (Natural Science Edition) > 2022 > 54(2): 70-75. > DOI: 10.6054/j.jscnun.2022028

CAO Kun, WANG Ruonan, XIONG Xingdong, WU Yun, LIU Xinguang. The Thermal Denaturation Conditions of β-galactosidase in Kluyveromyces lactis under Molecular Dynamics Simulation[J]. Journal of South China Normal University (Natural Science Edition), 2022, 54(2): 70-75. DOI: 10.6054/j.jscnun.2022028

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The Thermal Denaturation Conditions of β-galactosidase in Kluyveromyces lactis under Molecular Dynamics Simulation

1.
Guangdong Key Laboratory of Medical Molecular Diagnostics/Institute of Aging Research/Institute of Biochemistry & Molecular Biology, Guangdong Medical University, Dongguan 523808, China
2.
Scientific Research Platform Service Management Center, Guangdong Medical University, Dongguan 523808, China

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Received Date: June 21, 2021
Available Online: May 11, 2022

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Abstract

Abstract

To study the possible melting temperature of β-galactosidase in Kluyveromyces lactis, molecular dynamics (MD) simulations at four different temperatures (35, 50, 65 and 80 ℃) were performed for 50 ns, respectively. Then the conformational change of the enzyme and the difference of the enzyme active center were analyzed. The crucial information of temperature tolerance of β-galactosidase at the atomic level was revealed as follows: the overall conformation of β-galactosidase was the most stable at 35 ℃, which was the optimal temperature for enzyme activity; the atomic fluctuation of the enzyme increased significantly at 50 ℃, indicating that this temperature may approach the critical value of melting temperature; when the temperature was higher than 65 ℃, the structure of the protein lost its flexibility, which indicated that the protein had reached the melting temperature. Further conformational analysis showed that the microenvironment of β-D-galactopyranose (GAL) binding sites was destroyed at 80 ℃.
- molecular dynamics simulation,
- β-galactosidase,
- temperature,
- stability

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