DPE is a Glycan Tool Enzyme that catalyzes the reversible epimerization of D-fructose to D-psicose, a rare monosaccharide with 70% the sweetness of sucrose but negligible caloric content. This Epimerase belongs to the isomerase family and typically requires divalent metal cofactors for optimal activity. By interconverting the C3 hydroxyl group of ketohexoses, DPE plays a pivotal role in the biotechnological production of D-psicose, which has gained attention as a low-calorie sweetener and functional ingredient in food, pharmaceuticals, and health products due to its anti-obesity, anti-diabetic, and neuroprotective properties.

Fig. 1. Overview of DPE initial structure. (OA Literature) Fig.1 General overview of the initial structure.¹

DPE Production Service Overview

Are you currently facing challenges such as low conversion rates from fructose to allulose, thermal instability of biocatalysts, or difficulties in achieving purity for food-grade applications? Creative Biolabs' custom DPE production service helps you achieve high-yield rare sugar synthesis, obtain thermally robust enzymes, and streamline industrial biotransformations through our advanced Izumoring-based enzyme engineering and high-throughput expression platforms. We provide the precise biocatalytic tools needed to transform common feedstocks into high-value functional carbohydrates.

Explore How We Streamline Development Workflows

Custom DPE Production Workflow

Step 1

Enzyme Sourcing & In Silico Design

Leveraging our proprietary database of thoroughly characterized epimerases, we meticulously select an optimal scaffold for further development. This selection process is guided by computational modeling techniques that enable us to predict specific mutations aimed at enhancing the enzyme's catalytic efficiency. Through this in silico design approach, we strive to engineer enzymes with superior performance characteristics tailored to our specific needs.

Step 2

Expression System Optimization

Once the enzyme scaffold has been selected, we proceed to clone the target gene into high-efficiency vectors that are designed to maximize gene expression levels. Conversely, for research-grade applications that demand high yields and rapid turnaround times, we utilize optimized Escherichia coli systems that have been tailored to enhance protein production and solubility.

Step 3

Pilot Scale Fermentation

To evaluate the feasibility and efficiency of our enzyme production process, we conduct pilot-scale fermentations ranging from 5 liters to 50 liters in volume. These small-batch productions allow us to determine key performance metrics such as space-time yields and protein secretion efficiency, which are critical for scaling up the process to industrial levels. By closely monitoring these parameters, we identify potential bottlenecks and optimize the fermentation conditions accordingly.

Step 4

Characterization & Immobilization

Following fermentation, the enzyme undergoes rigorous testing to assess its thermal stability and metal-ion dependency, which are essential for understanding its behavior under various operational conditions. Subsequently, we employ custom immobilization techniques that are specifically designed to enhance the enzyme's recyclability and stability, thereby extending its useful lifetime and reducing operational costs. These immobilization methods may include covalent attachment to solid supports, encapsulation within polymeric matrices, or cross-linking with bifunctional reagents.

Step 5

Scaling & Downstream Processing

Once the enzyme has been fully characterized and immobilized, we proceed to scale up the production process to meet the required demand. This involves large-scale fermentation runs followed by high-purity purification steps to remove any impurities or contaminants. Depending on the intended application, the purified enzyme may then be lyophilized for long-term storage and ease of transportation.

Fig. 2. DPE production workflow. (Creative Biolabs AI) Fig.2 DPE manufacturing workflow.

Why Choose Us?

Expert-Led Enzyme Engineering
Our team specializes in designing custom DPE variants with enhanced thermal stability, catalytic efficiency, and substrate specificity using advanced directed evolution and protein engineering tools. Whether you need a variant optimized for high-temperature reactions or improved activity with alternative substrates, we deliver solutions tailored to your process requirements.

Scalable Fermentation & Purification
From lab-scale to industrial production, we leverage optimized microbial expression systems and cost-effective downstream purification processes to ensure high yields of ultra-pure DPE.

End-to-End Customization
We collaborate closely with clients to refine enzyme properties, including metal cofactor preferences, pH tolerance, and reaction kinetics, ensuring seamless integration into your existing workflows for D-psicose synthesis or rare sugar production.

Proven Track Record in Rare Sugar Applications
With years of experience supplying DPE for food, pharmaceutical, and biotech industries, we understand the nuances of producing low-calorie sweeteners, bioactive precursors, and metabolic research tools. Our enzymes consistently meet stringent performance benchmarks.

Customer Reviews

Custom DPE Benefit
"Using custom DPE in our research has significantly facilitated the development of high-temperature biotransformation protocols. The exceeding allowed us to operate without the constant fear of enzyme denaturation."- 1 year ago, Dr. A***n L***e.

Immobilization Advantage
"The immobilization service provided by Creative Biolabs significantly improved our space-time yields. Compared to free-enzyme alternatives, the recyclability of the DP made our rare sugar production economically feasible at a pilot scale."- 6 months ago, Prof. M***o S***z.

Working Together to Bring Innovations to Market Faster

FAQs

Q: What is the typical conversion rate I can expect using your DPE?

A: Under optimized conditions, our DPEs achieve an equilibrium conversion of approximately 25-32% from D-fructose. We further optimize this by adjusting metal-ion concentrations depending on your application.

Q: Can you provide enzymes that are safe for food production?

A: Yes. We specialize in using Bacillus subtilis and other microbial hosts. We provide the necessary documentation to support your regulatory filings for food-grade rare sugar production.

Q: How does immobilization affect the activity of the epimerase?

A: While immobilization can sometimes slightly reduce initial specific activity, it dramatically increases the half-life and allows for enzyme recovery. Our proprietary matrices are designed to minimize steric hindrance, maintaining high catalytic efficiency over multiple cycles.

Q: How do I know which variant is best for my project?

A: Our PhD-level consultants will analyze your project goals and suggest the most appropriate scaffold. Please contact our team for a technical feasibility assessment to determine the ideal enzyme profile for your needs.

Extended Services

Custom D-Psicose Production Service

We specialize in tailored enzymatic synthesis of D-psicose, leveraging advanced biocatalysts to deliver high-purity, cost-effective rare sugars.

Glycan Modification and Labeling Services

Our expert team provides precision glycan engineering and isotopic/fluorescent labeling services, enabling detailed structural analysis and functional studies of carbohydrates.

How to Contact Us

Creative Biolabs provides end-to-end solutions for the design, optimization, and large-scale production of DPE. We deliver customized biocatalysts tailored to your specific temperature, pH, and substrate concentration requirements, ensuring that your transition from laboratory pilot to metric-ton manufacturing is seamless and economically viable. For detailed technical specifications, pricing, and project timelines, please reach out to our global support team.

Reference

Li, Congcong, et al. "A possible mechanism of graphene oxide to enhance thermostability of D-psicose 3-epimerase revealed by molecular dynamics simulations." International Journal of Molecular Sciences 22.19 (2021): 10813. Distributed under Open Access license CC BY 4.0, without modification. https://doi.org/10.3390/ijms221910813.

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