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This research introduces MI-PEFT, a parameter-efficient fine-tuning framework that leverages protein language models to accurately identify acidophilic proteins despite significant dataset class imbalances. By integrating Mixture-of-Experts with LoRA techniques on the ESM backbone, the method offers a computationally efficient alternative to traditional experimental screening for industrial biocatalysis applications.
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MI-PEFT: Mixture-of-Experts Integrated Parameter-Efficient Fine-Tuning Protein Language Models Improves Acidophilic Proteins Classification

arXiv2 min read

arXiv:2609.08059v1 Announce Type: cross Abstract: Acidophilic proteins that remain stable and functional under highly acidic conditions, are important for industrial biocatalysis, acid-related bioprocessing, and the discovery of acid-stable enzymes. However, their identification relies heavily on time-consuming experimental screening methods. With the rapid growth of protein sequence databases, the need for computational identification methods that are both accurate and efficient has become stronger. The emergence of protein language models (PLMs) has significantly improved the sequence representation of downstream biological prediction tasks. This paper proposes MI-PEFT, a mixture-of-experts integrated parameter-efficient fine-tuning framework. Built on the ESM C-600M backbone, the framework incorporates LoRA-based PEFT methods and a DeepSeekMoE-based classification head to resolve the limitations of PEFT and significantly improve computational efficiency. Notably, this task is characterized by a significant class imbalance in the dataset, making high specificity particularly challenging. The experimental results demonstrate that MI-PEFT on PLMs, especially {\text{C}}^{\text{3}}\text{A}, serves as an efficient tool for identifying acidophilic proteins and a constrained pathway that helps resolve class-imbalance by preserving the pretrained representations.

Abstract:Acidophilic proteins that remain stable and functional under highly acidic conditions, are important for industrial biocatalysis, acid-related bioprocessing, and the discovery of acid-stable enzymes. However, their identification relies heavily on time-consuming experimental screening methods. With the rapid growth of protein sequence databases, the need for computational identification methods that are both accurate and efficient has become stronger. The emergence of protein language models (PLMs) has significantly improved the sequence representation of downstream biological prediction tasks. This paper proposes MI-PEFT, a mixture-of-experts integrated parameter-efficient fine-tuning framework. Built on the ESM C-600M backbone, the framework incorporates LoRA-based PEFT methods and a DeepSeekMoE-based classification head to resolve the limitations of PEFT and significantly improve computational efficiency. Notably, this task is characterized by a significant class imbalance in the dataset, making high specificity particularly challenging. The experimental results demonstrate that MI-PEFT on PLMs, especially {\text{C}}^{\text{3}}\text{A}, serves as an efficient tool for identifying acidophilic proteins and a constrained pathway that helps resolve class-imbalance by preserving the pretrained representations.

Quantitative Methods (q-bio.QM); Machine Learning (cs.LG)

arXiv:2609.08059 [q-bio.QM]

(or arXiv:2609.08059v1 [q-bio.QM] for this version)

https://doi.org/10.48550/arXiv.2609.08059 Focus to learn more arXiv-issued DOI via DataCite (pending registration)

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Full text under the publisher's open licence · 260 words

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