CD Biosynsis can help our customers overcome challenges in lipase production by leveraging emerging technologies in synthetic biology to meet the growing demand for lipases in scientific research, industrial production, medical diagnostics, and so on. We are committed to breaking the limitations of lipase in large-scale production and traditional industrial applications and developing more time- and cost-effective methods of lipase production to advance the use of lipase in a wide range of applications.
Advantages of Synthetic Biology-Driven Lipase Production
Lipases also known as triacylglycerol acylhydrolases EC. 3.1.1.3, are hydrolases capable of catalyzing the hydrolysis of triacylglycerols (TAGs) into glycerol and fatty acids (FAs) and can be produced by bacteria, fungi, plants and mammals. However, there are many limitations in the current production process of lipase and its industrial application, such as low yield, poor thermal stability and activity. On the other hand, improvement of lipases by conventional cloning, expression and identification methods is considered to be expensive and inefficient. Recent advances in synthetic biology can provide a framework for developing methods that can accurately predict and optimize different factors of enzyme activity and can help us to efficiently develop quality lipase producing microorganisms. Recent advances in synthetic biology can provide a framework for the development of methods that can accurately predict and optimize different factors of lipase activity, thus helping us to efficiently develop quality lipase producing microorganisms.
Figure 1. Full length lipase structure. (Khan MT, et al., 2020)
What We Provide
CD Biosynsis' advanced synthetic biology platform and extensive expertise allows us to help our customers develop customized and effective strategies to achieve improved production of proteases.
Featured Services
- Identification and characterization of novel lipases with higher stability and activities.
- Chemical modification of lipases to enhance their productivity, stability, and catalytic performance.
- Design and engineering of lipases to generate new variants with improved properties such as substrate specificity and stereoselectivity.
- Production of nanomaterial-immobilized lipases for improved stability, enzyme activity, and recyclability.
- Isolation, identification, and optimization of lipase-producing strains to enhance lipase production.
Key Strategies and Technologies
Deliverables
- Lipase-producing microorganisms.
- High-quality bacterial and fungal lipases.
How We Can Help
CD Biosynsis' advanced technology and expertise in synthetic biology can help our customers overcome any difficulties they may encounter in lipase production. Our scientists can establish a synthetic biology-based workflow for improving biological processes to help enhance the performance of lipase-producing microorganisms or improve the catalytic activity and stability of lipases.
Engineering of Microbial Chassis for Improved Lipase Production
We have collected a variety of microbial strains that have the potential to be developed as powerful synthetic biology chassis. Our scientists can help our customers develop effective strategies for synthetic biology chassis engineering to obtain ideal microbial chassis with improved properties and high lipase producing capacity. The following is a list of our collection of microbial strains used for lipase production. If you are interested in other microbial strains, please fill out the online inquiry form and tell us more about your project.
| Burkholderia ubonensis |
Staphylococcus warneri |
Bacillus sp. |
Serratia marcescens |
Enterococcus faecium |
| Acinetobacter sp. |
Penicillium sp. |
Trichoderma harzianum |
Rhodotorula glutinis |
Sporidiobolus pararoseus |
| Candida cylindracea |
Talaromyces thermophilus |
Geotrichum candidum |
Debaryomyces hansenii |
Aureobasidium pullulans |
Lipase Improvement Strategies Based on Synthetic Biology
- Using advanced computational analysis and engineering tools combined with synthetic biology strategies to optimize lipases and improve their properties such as thermal stability, pH tolerance, substrate selectivity, and catalytic activity.
- Using a robust technology platform based on synthetic biology, microbial cell factories for efficient lipase production can be constructed to achieve reduced by-product formation, increased flux in metabolic pathways, and improved enzyme catalytic efficiency.
Applications of Lipase
CD Biosynsis is committed to enhancing the function and yield of microbial lipases using advanced synthetic biology techniques to meet the growing demand in a variety of applications.
Applications of lipase in the food industry
- Used in the production of dairy products, baked goods, and fruit juices.
- Used in the esterification of fats and oils to produce modified acylglycerols.
Applications of lipase in the pharmaceutical industry
- Used in the treatment of cardiovascular disease, obesity, anxiety, inflammation, and pain.
- Used in the preparation of optically active compounds, such as pure alcohols, amines, and carboxylic acids.
Application of lipase in bioremediation
- Used in bioremediation of wastewater containing fats, oils, and proteins.
Application of lipase in the leather and fur industry
- Used in pigskin degreasing to make the leather soft and easy to dye.
Want to Learn More?
As a rapidly growing synthetic biology company, CD Biosynsis is committed to helping our customers meet the growing and evolving demand for industrial enzyme production. All of our deliverables will undergo a rigorous quality testing process to ensure the quality and reliability and can be delivered on time. If you are interested in our services or have any further questions, please do not hesitate to contact us.
References
- Khan MT, et al. Characterization and synthetic biology of lipase from Bacillus amyloliquefaciens strain. Arch Microbiol, 2020, 202(6): 1497-1506.
- Gamboa-Melendez H, et al. Synthetic Biology to Improve the Production of Lipases and Esterases (Review). Methods Mol Biol, 2018;1835: 229-242.
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