Invented by Andreas W. Schirmer, Haibo Wang, Stephen B. del Cardayre, Zhihao Hu, Louis G. Hom, Baolong Zhu, Cindy Chang, Emanuela E. Popova, Genomatica Inc

The market for methods for producing omega-hydroxylated fat acid derivatives is rapidly growing as the demand for these compounds continues to rise. Omega-hydroxylated fat acid derivatives are a type of fatty acid derivative that possess hydroxyl groups at the omega carbon position, which is the carbon furthest away from the carboxyl group. These compounds have gained significant attention due to their potential health benefits and various applications in industries such as pharmaceuticals, cosmetics, and food. Omega-hydroxylated fat acid derivatives are known for their anti-inflammatory, anti-cancer, and anti-oxidant properties, making them highly sought after in the market. One of the key drivers for the increasing demand for omega-hydroxylated fat acid derivatives is the growing consumer awareness of the importance of a healthy diet and the role of these compounds in promoting overall well-being. These derivatives are commonly found in fish oil, which is known for its high omega-3 fatty acid content. However, the extraction of omega-hydroxylated fat acid derivatives from natural sources can be expensive and time-consuming. To meet the rising demand, researchers and companies are actively developing new methods for producing omega-hydroxylated fat acid derivatives. These methods aim to provide a cost-effective and sustainable solution for obtaining these compounds. One such method involves the use of microbial fermentation, where specific microorganisms are engineered to produce omega-hydroxylated fat acid derivatives through metabolic pathways. Another approach involves the chemical synthesis of these derivatives using various catalysts and reactants. This method allows for greater control over the production process and can be scaled up to meet commercial demands. However, it is important to ensure that the chemical synthesis methods are environmentally friendly and do not pose any risks to human health. The market for methods for producing omega-hydroxylated fat acid derivatives is highly competitive, with numerous companies and research institutions actively involved in developing innovative techniques. These methods not only focus on improving the efficiency and cost-effectiveness of production but also aim to enhance the quality and purity of the derivatives. In addition to the pharmaceutical and cosmetic industries, the food industry is also a significant consumer of omega-hydroxylated fat acid derivatives. These compounds are used as functional ingredients in various food products, including dietary supplements, functional beverages, and fortified foods. The growing trend of incorporating healthy ingredients in food products has further fueled the demand for omega-hydroxylated fat acid derivatives. As the market for these derivatives continues to expand, it is crucial for manufacturers to ensure compliance with regulatory standards and maintain high-quality standards. This includes conducting thorough testing and analysis to ensure the safety and efficacy of the derivatives. In conclusion, the market for methods for producing omega-hydroxylated fat acid derivatives is experiencing significant growth due to the increasing demand for these compounds in various industries. The development of innovative and sustainable production methods is crucial to meet the rising demand and ensure the availability of high-quality derivatives. With ongoing research and advancements in technology, the market for omega-hydroxylated fat acid derivatives is expected to continue its upward trajectory in the coming years.

The Genomatica Inc invention works as follows

The disclosure is related to omega-hydroxylated fat acid derivatives, and their production methods. The disclosure includes a novel, environmentally-friendly production method for omega-hydroxylated fat acid derivatives with high purity and yield. Recombinant microorganisms are also included that produce omega-hydroxylated fat acid derivatives by selective fermentation.

Background for Methods for producing omega-hydroxylated fat acid derivatives

Definitions

EXAMPLES

Example 2: Production of?-Hydroxy fatty acid derivatives from Recombinant E. coli

Example 2 : Analysis of? -Hydroxylated fatty acid derivatives

Example 3″: Conversion from dodecanoic to 12(? “Example 3: Conversion of dodecanoic to 12(?

Example 4 : Conversion of Dodecanoic Acid into 12(? “Example 4: Conversion of Dodecanoic Acid to 12(?

Example 5. Conversion of Fatty Acid derivatives into?-Hydroxylated fatty acid derivatives by an E. coli strain expressing a hybrid cyp153A – Red450RhF fusion protein

Example 6 : Production of?-Hydroxylated fatty acid derivatives from Glucose using Recombinant E. coli strains expressing a CYP153A – Red450RhF hybrid fusion protein

Example 7. Production ?,?-Diacids by a Recombinant E. coli strain

Example 8 : Production of Subterminally Hydrogenated Fatty Acids By E. coli strains expressing cyp102A1 expressed from Bacillus Megaterium

Example 10: Efficient Production of?-1-,?-2- and?-3?-Hydroxylated fatty acids from Glucose By E. coli strains Expressing cyp102A7 From Bacillus licheniformis

Example 10 – Production ?,?-Diesters by Recombinant E. coli strains from Glucose

Example 12: Production of?-Amino Acid Derivatives by Recombinant E. coli strains

Example 12 – Production of? -Hydroxylated fatty acid derivatives from Diverse feedstocks

Example 14: Production of?-Hydroxylated fatty acid derivatives from Glucose using Recombinant E. coli strains expressing Various CYP153A Reduced Fusion Proteins”.

Example 15: Strain and Plasmid Construct for Library Screenings

Example 15: Saturation Libraries of the P50 Catalytic Domain of cyp153A(G307A)-Red450RhF Fusion Protein

Example 16: Partial Site Saturation Libraries of the Reductase Domain of CYP153A(G307A)-Red450RhF Fusion Protein

Example 17: Combinatorial Library of the Reductase Domain of CYP153A(G307A)-Red450RhF Fusion Protein

Example 18: Combinatorial Library of the Catalytic and Reductase Domain of CYP153A(G307A)-Red450RhF Fusion Protein

Example 19. Site Saturation Mutagenesis at Positions 141 and 309 in CYP153A (G307A A796V), Red450RhF

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