BACKGROUND AND OBJECTIVES: Corynebacterium glutamicum has emerged as a safe and efficient host for recombinant protein production, gaining prominence in biopharmaceutical and industrial applications. Its ability to utilize alternative carbon sources, such as acetate, significantly reduces production costs. Moreover, its endotoxin-free nature, adaptability to large-scale conditions, and capacity for direct protein secretion enhance its appeal. However, challenges remain, including limited expression of certain proteins and its thick cell wall, which can hinder secretion efficiency. This study examines the key attributes that make C. glutamicum an effective host, while also addressing its limitations, aiming to provide insights into optimizing its use for industrial protein production. MATERIALS AND METHODS: the present narrative review is based on published scientific articles from 1995 to 2024, in PubMed, Google Scholar, and ScienceDirect using key terms such as "Corynebacterium glutamicum", "Recombinant protein", and " Corynebacterium glutamicum AND Recombinant protein". RESULTS AND DISCUSSION: Corynebacterium glutamicum is a promising host for recombinant protein production, offering non-pathogenic, endotoxin-free advantages and efficient protein secretion, reducing purification costs. Its low extracellular protease activity enhances protein stability, and its ability to utilize inexpensive carbon sources like acetate makes it ideal for industrial applications. However, limitations such as its thick cell wall and restricted protein secretion necessitate optimization. Strategies like strong promoters, engineered signal peptides, and Sec/Tat pathways have improved secretion efficiency. Additionally, its robust growth and stress tolerance ensure stable, scalable bioprocessing, reinforcing its potential as an optimized platform for industrial biotechnology.
