Lipases, a broad and versatile class of serine hydrolases, catalyze the hydrolysis and formation of ester bonds in both aqueous and non-aqueous environments. Unlike many other enzyme classes requiring specific cofactors or metal ions, lipases operate cofactor-independently, simplifying reaction design and enhancing process stability. Their structural robustness and tolerance to organic solvents make them highly adaptable and reliable catalysts for industrial biotransformations under a wide range of reaction conditions.

Typically derived from microbial or fungal sources, lipases are expressed extracellularly, facilitating straightforward recovery and purification from fermentation media. They are widely recognized for catalyzing reactions such as esterification, transesterification, and interesterification, alongside hydrolysis, often under mild conditions and at ambient temperature and pressure. Their ability to accept diverse substrates while maintaining high enantio-, regio-, and chemoselectivity allows them to perform complex transformations that are difficult to achieve through traditional chemical synthesis.

On an industrial scale, lipase-catalyzed processes have been extensively demonstrated, including large-scale production of biodiesel, chiral intermediates, and specialty esters. Fermentation and immobilization technologies have enabled production yields exceeding hundreds of kilograms of active enzyme. This scalability, combined with operational simplicity and high catalytic efficiency, positions lipases as essential tools for sustainable, efficient, and selective synthesis across the pharmaceutical, food, and chemical industries.

Aminoverse’s lipase enzyme panel 9 beta-kit now includes a selection of nine free lipases in mg scale: BTL2 Bacillus thermocatenulatus, CALA Candida antarctica, CALB Candida antarctica + 1 variant, CTL Candida tenuis, RML Rhizomucor miehei + 1 variant, ROL Rhizopus oryzae, and TLL Thermomyces lanuginosus. Aminoverse can also support customized screening to identify optimal enzymes for your specific applications.

The Aminoverse immobilized lipase panel expands the capabilities of modern biocatalysis, providing a reliable set of seven immobilized lipases optimized for diverse synthetic transformations. Unlike free enzymes, immobilized lipases exhibit enhanced stability, tunable selectivity, and improved tolerance to challenging reaction conditions. Their immobilized form allows operation in organic solvents, elevated temperatures, and continuous-flow systems, enabling process configurations that are inaccessible to soluble enzymes.

Recombinantly expressed in Pichia pastoris, these lipases offer high purity and consistent performance, minimizing undesired side reactions in reactions such as ester hydrolysis, esterification, transesterification, and aminolysis. Preliminary evaluations have revealed that three variants in the kit are not currently available on the market in immobilized form, while another demonstrates superior activity compared with the present industrial benchmark. Such results highlight their potential for efficient, selective, and sustainable synthesis across both research and manufacturing settings.

Developed in collaboration with Bisy and ChiralVision, this kit represents a robust, industrially scalable platform for screening, process development, and production.

Aminoverse’s immobilized lipase enzyme panel 7 beta-kit includes a selection of seven immobilized lipases in mg scale: BTL2 Bacillus thermocatenulatus, CALB Candida antarctica variant, CRL3 Candida rugosa, CRL4 Candida rugosa, CTL Candida tenuis, RML Rhizomucor miehei, and TLL Thermomyces lanuginosus. Aminoverse can also support customized screening to identify optimal enzymes for your specific applications.