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Multi-level Integrated Engineering Enhances Neutral β-Glucanase Production in Komagataella phaffii.

Hai Xu1, Xiaowei Shao1, Yuzhe Peng1

  • 1School of Biotechnology and Key Laboratory of Industrial Biotechnology of Ministry of Education, Jiangnan University, 1800 Lihu Road, Wuxi 214122, China; National Engineering Research Center of Cereal Fermentation and Food Biomanufacturing, Jiangnan University, 1800 Lihu Road, Wuxi 214122, China; Jiangsu Provincial Research Center for Bioactive Product Processing Technology, Jiangnan University, 1800 Lihu Road, Wuxi 214122, China.

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|April 18, 2026
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Summary

We engineered Komagataella phaffii to produce neutral β-1,3-glucanase (BgA) efficiently. This enhanced enzyme production overcomes industrial limitations, making BgA more accessible for food applications.

Keywords:
Biobrick assembly systemK. phaffiiTranscription regulationTranslation regulationβ-glucanase

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Area of Science:

  • Biotechnology
  • Enzyme Engineering
  • Industrial Microbiology

Background:

  • Neutral β-1,3-glucanase (BgA) is crucial in food processing (brewing, baking, juice clarification).
  • Current industrial BgA production faces challenges with low secretion and high costs.

Purpose of the Study:

  • To develop an efficient, scalable production system for neutral β-1,3-glucanase (BgA) using Komagataella phaffii.
  • To overcome limitations of low secretion titers and high production costs for industrial BgA application.

Main Methods:

  • Established a multi-layered engineering framework in K. phaffii.
  • Screened promoter and signal peptide libraries for optimal secretion.
  • Implemented synergistic transcriptional and translational regulation strategies.
  • Validated industrial scalability through fed-batch fermentation.

Main Results:

  • Identified PDAS1 and MFα signal peptide for optimal BgA secretion (5.5 U/mL·OD600).
  • Co-overexpression of Mxr1 and Mit1 increased BgA titers by 72%.
  • Engineering the translation initiation complex yielded a 1.9-fold increase in BgA production.
  • Achieved a final BgA titer of 1.1 g/L in a 5-L bioreactor.

Conclusions:

  • Demonstrated a robust, integrated engineering strategy for BgA production.
  • Successfully established K. phaffii as a competitive host for neutral β-glucanase production.
  • Resolved secretory bottlenecks, paving the way for cost-effective industrial enzyme application.