Translational Modification and pH Optimization of Expression Media for High-Yield Recombinant Human-like Collagen (RHC) Production in Pichia pastoris GS115

DOI: 10.22161/ijeab.105.17

Abstract:
Collagen plays a vital role in maintaining tissue structure and promoting repair, making it a key component of the extracellular matrix. Due to the limitations associated with extracting collagen from animal sources, interest in recombinant human-like collagen (RHC) has grown substantially. This study presents an approach to enhance RHC production in Pichia pastoris GS115 by engineering a novel plasmid (pPIC9K-OSTI/RHC) and refining fermentation parameters. Among the tested conditions, a pH of 6 was found to be optimal, resulting in an RHC high yield of 0.35 g/L. The use of the OSTI α-signal peptide notably improved secretion efficiency, contributing to increased protein output. This work demonstrates a scalable and cost-effective strategy for producing recombinant human-like collagen, laying the groundwork for future applications in tissue engineering, wound healing, and biomedical research.

Keywords:
Recombinant Human-Like Collagen (RHC), Pichia pastoris, OSTI signal peptide, pH optimization, Protein expression.

Article Info:
Received: 05 Sep 2025; Received in revised form: 03 Oct 2025; Accepted: 07 Oct 2025; Available online: 15 Oct 2025

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