Modeling enzyme temperature stability from sequence segment perspective
Abstract
Developing enzymes with desired thermal properties is crucial for a wide range of industrial and research applications, and determining temperature stability is an essential step in this process. Experimental determination of thermal parameters is labor-intensive, time-consuming, and costly. Moreover, existing computational approaches are often hindered by limited data availability and imbalanced distributions. To address these challenges, we introduce a curated temperature stability dataset designed for model development and benchmarking in enzyme thermal modeling. Leveraging this dataset, we present the \textit{Segment Transformer}, a novel deep learning framework that enables efficient and accurate prediction of enzyme temperature stability. The model achieves state-of-the-art performance with an RMSE of 24.03, MAE of 18.09, and Pearson and Spearman correlations of 0.33, respectively. These results highlight the effectiveness of incorporating segment-level representations, grounded in the biological observation that different regions of a protein sequence contribute unequally to thermal behavior. As a proof of concept, we applied the Segment Transformer to guide the engineering of a cutinase enzyme. Experimental validation demonstrated a 1.64-fold improvement in relative activity following heat treatment, achieved through only 17 mutations and without compromising catalytic function.
Keywords
Cite
@article{arxiv.2507.19755,
title = {Modeling enzyme temperature stability from sequence segment perspective},
author = {Ziqi Zhang and Shiheng Chen and Runze Yang and Zhisheng Wei and Wei Zhang and Lei Wang and Zhanzhi Liu and Fengshan Zhang and Jing Wu and Xiaoyong Pan and Hongbin Shen and Longbing Cao and Zhaohong Deng},
journal= {arXiv preprint arXiv:2507.19755},
year = {2025}
}