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Endospores and Sporulation

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Endospores are specialized, dormant cells primarily formed by Gram-positive bacteria, including Bacillus and Clostridium, enabling survival under extreme environmental conditions. Due to their unique composition and formation process, these structures are highly resistant to physical and chemical insults, such as extreme heat, ultraviolet and ionizing radiation, desiccation, and toxic chemicals. Rare instances of endospore-like structures have also been observed in some Gram-negative bacteria,...

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Updated: Mar 13, 2026

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes

Published on: November 7, 2012

Engineering CotA Laccase for Acidic pH Stability Using Bacillus subtilis Spore Display.

Silu Sheng¹, Han Jia¹, Sidney Topiol²

¹New Jersey Institute of Technology, Department of Chemistry and Environmental Science, University Heights, Newark, NJ 07102, USA.

Journal of Microbiology and Biotechnology

|October 27, 2016

Summary

This summary is machine-generated.

Bacillus subtilis spores enable robust protein display for enhanced biocatalysis. Engineered CotA variants show improved pH stability and increased product yield, overcoming limitations of traditional methods.

Keywords:

Protein display directed evolution laccase protein stability spore

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Spore Adsorption as a Nonrecombinant Display System for Enzymes and Antigens

Spore Adsorption as a Nonrecombinant Display System for Enzymes and Antigens

Published on: March 19, 2019

Area of Science:

Biotechnology
Enzyme Engineering
Protein Engineering

Background:

Traditional protein display methods face challenges with protein folding and cell viability.
Bacillus subtilis spores offer a stable and viable platform for protein immobilization, maintaining genotype-phenotype linkage.
Spore-based display leverages natural sporulation and chaperone systems to facilitate correct protein folding.

Purpose of the Study:

To engineer CotA as a whole-cell biocatalyst with improved pH stability using Bacillus subtilis spore display.
To enhance the operational stability and reusability of the CotA biocatalyst for industrial applications.

Main Methods:

Screening of a library of approximately 3,000 Bacillus subtilis clones displaying CotA variants.
Directed evolution and site-directed mutagenesis to identify and combine beneficial mutations for improved pH stability.
Characterization of wild-type (wt) CotA and engineered variants (E498G, T480A/E498G) for activity, stability, and reusability.

Main Results:

A single mutation (E498G) significantly increased the half-life of CotA at pH 4 by 24.8-fold compared to wt-CotA.
A double mutant (T480A/E498G) exhibited a 62.1-fold greater half-life at pH 4 than wt-CotA.
Engineered CotA variants (E498G and T480A/E498G) demonstrated 3.7- and 5.3-fold higher product yields, respectively, after seven recycling cycles over 42 hours.

Conclusions:

Bacillus subtilis spore display is an effective strategy for enhancing enzyme pH stability and biocatalytic performance.
Engineered CotA variants exhibit superior operational stability and reusability, making them promising for industrial biocatalysis.
This approach overcomes limitations of traditional protein display, offering a robust platform for enzyme engineering.