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ORIGINAL RESEARCH article

Front. Nutr.
Sec. Nutrition and Food Science Technology
Volume 11 - 2024 | doi: 10.3389/fnut.2024.1505584
This article is part of the Research Topic Application of Enzyme Biotechnology in Food and Health Products View all articles

Modification of the active centre of nattokinase to enhance its thermostability using a strategy based on molecular dynamics simulation, steered dynamics simulation and conservative prediction

Provisionally accepted
Li Yuan Li Yuan Zhu Wenhui Zhu Wenhui Chen Liangqi Chen Liangqi Tang Xiyu Tang Xiyu Ma Aixia Ma Aixia Ma Yuwei Ma Yuwei Li Tongli Li Tongli Li Xinrui Li Xinrui *Ye Ma Ye Ma Jinyao Li Jinyao Li
  • Xinjiang University, Urumqi, China

The final, formatted version of the article will be published soon.

    The poor thermostability of nattokinase represents a significant limitation in its potential applications. Additionally, there is a notable absence of studies focused on modifying residues within the active site region of nattokinase with the aim of enhancing its catalytic properties. Furthermore, the direct utilisation of directed evolution often yields unfavourable outcomes, with a considerable workload being a common consequence. In this study, a novel combined approach was proposed, based on molecular dynamics simulation, steered dynamics simulation and conservative analysis with site-directed mutagenesis, with the aim of addressing the aforementioned issue. Based on these findings, the mutant A216K was selected for a 5.7-fold increase in half-life at 55°C with a small increase in activity, which further enhanced the mutation library of the thermal stability enhancement site in the enzyme's active centre. We also used molecular dynamics simulations to elucidate the mechanism by which three mutants of 216 amino acid residues (A216E, A216K and A216R) increase the thermostability of nattokinase. It is anticipated that this strategy will provide novel insights into enzyme engineering research.

    Keywords: Nattokinase, thermostability, Active center region, rational design, molecular dynamics

    Received: 03 Oct 2024; Accepted: 28 Oct 2024.

    Copyright: © 2024 Yuan, Wenhui, Liangqi, Xiyu, Aixia, Yuwei, Tongli, Xinrui, Ma and Li. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

    * Correspondence: Li Xinrui, Xinjiang University, Urumqi, China

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