Broadest Pichia pastoris protein expression platform

VTU Technology’s Pichia pastoris system provides one of the most powerful and multifaceted recombinant protein expression and production technology platforms holding world productivity records for Pichia-derived recombinant proteins.

Since its foundation 2008, VTU has continuously optimized and expanded its Pichia technology to form an expression toolbox of unparalleled versatility and flexibility for the fast track generation of high performance Pichia pastoris protein production strains and economically viable protein production processes for biopharmaceuticals and other proteins.

Technology base

VTU’s technology suite is based on a cutting-edge Pichia pastoris protein production platform based on its exclusive 1st and 2nd generation AOX1 promoter libraries. These enable sensitive fine-tuning of gene expression by selecting the perfect match out of a huge possible range of promoter/target gene combinations.

The company´s AOX1 promoter libraries control the expression of target genes under two applicable cultivation regimes:

• VTU´s 1st generation AOX1 promoter library enables unprecedented yields of target protein of more than 20 g/L by secretion into the culture medium upon methanol (MeOH)induction.
• VTU´s 2nd generation methanol-free AOX1 promoter library functions by derepression even with just glycerol or glucose as the sole carbon source. While retaining high expression levels of up to 15 g/L the use of toxic and explosive methanol as a substrate is completely obviated. Additional major advantages of this new breakthrough technology are reduced oxygen consumption and therefore significantly reduced heat production and cooling effort in bioreactor cultivations as well as a significant potential to reduce process time and cost of goods.

The versatility and effectiveness of VTU´s Pichia system is further underlined by a set of proprietary expression enhancing helper factors, several platform strains with different genetic backgrounds, elaborated cloning and transformation protocols, a high-throughput micro-scale screening and cultivation regime and effective fermentation protocols for maximization of product yield and overall process performance.

Capacities for cultivation and analysis of up to 25.000 clones per week in 96-deep well plates enable the development of customized high performance expression strains with unmatched product yields in minimum time.

With the addition of RCT’s Pichia GlycoSwitch® system for homogeneous N-glycosylation, the VTU portfolio also encompassesa new dimension of recombinant protein expression, creating a high performance production platform for recombinant homogeneous glycoproteins with Man5 and other human-like glycans.

Advantages

VTU´s Pichia pastoris expression system is ideally suited for high-level expression of recombinant proteins for therapeutic or industrial applications, offering many advantages.

These include:

• A broader platform offering manifold expression and production strategies to meet highly specific expression needs
• High production levels for a wide range of biologics and other proteins with yields of more than 20 g/L of secreted target protein from MeOH induced processes
• Up to 15 g/L of secreted target protein from 2nd generation MeOH-free processes that use glycerol or glucose as the sole carbon source, with significantly less heat formation and cooling demand furnishing safe and economically viable production processes
• Outstanding recombinant glycoprotein product yields and controlled GlcNAc2Man5-pattern or generation of other human-like glycoforms
• Tight development timelines
• Competitive production processes

Services

VTU offers a suite of services including:

• High-speed Pichia pastoris expression strain development
• Fermentation process development and optimization
• Downstream and analytical process development
• Small-scale production of purified non-GMP proteins
• Sound technology & data transfer to customers
• Out licensing opportunities for:
  • Human serum albumin and Human serum transferrin
  • HSA-fusion proteins
  • Cell culture proteins