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Recombinant DNA

Recombinant DNA

Production of Pharmaceuticals

Production of Pharmaceuticals

Industrial insulin production uses genetically engineered E. coli expressing a proinsulin gene controlled by a tryptophan promoter and containing a methionine linker for later cleavage. The cells also carry ampicillin resistance for selective growth. Seed cultures are stored at −80 °C and production begins by thawing a small amount to inoculate starter cultures, which are progressively scaled to a 50,000-L bioreactor. In the bioreactor, E. coli grow in nutrient-rich media under sterile, tightly...

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Related Experiment Video

Updated: Jul 12, 2026

Expression of Recombinant Proteins in the Methylotrophic Yeast Pichia pastoris

Expression of Recombinant Proteins in the Methylotrophic Yeast Pichia pastoris

Published on: February 26, 2010

[Recombinant batroxobin expressed highly in Pichia pastoris].

Zhao-Fa Li¹, Xue-Ling Yu, Jin-Lu Huang

¹Institute of Bioengineering, Academy of Military Medical Science, Beijing 100071, China.

Sheng Wu Gong Cheng Xue Bao = Chinese Journal of Biotechnology

|June 21, 2007

Summary

Recombinant batroxobin was successfully produced in Pichia pastoris yeast. This engineered snake venom enzyme shows potential as a novel hemostatic agent for controlling bleeding.

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Area of Science:

Biotechnology
Molecular Biology
Protein Expression

Context:

Snake venom enzymes, like batroxobin, are valuable for their hemostatic properties.
Traditional production methods face challenges in yield and purity.
Recombinant protein expression offers a scalable and controlled production alternative.

Purpose:

To establish a technology route for producing recombinant batroxobin using Pichia pastoris.
To characterize the expressed and purified recombinant batroxobin.
To evaluate the hemostatic efficacy of recombinant batroxobin in vitro and in vivo.

Summary:

The batroxobin gene was synthesized and cloned into the pPIC9 vector.
The recombinant plasmid was transformed into Pichia pastoris GS115 for expression.
Purified recombinant batroxobin (30.55 kD) demonstrated specific activity (238 NIH units/mg) and effectively converted fibrinogen to fibrin, shortening bleeding time in vivo.

Impact:

This study provides a foundational method for developing recombinant snake venom thrombin-like enzymes.
The successful production of functional recombinant batroxobin paves the way for novel hemostatic therapies.
Establishes a scalable biotechnological approach for producing therapeutic snake venom proteins.