The IPB has once again been recognized for its exemplary actions in terms of equal opportunity-oriented personnel and organizational policies and has received the TOTAL E-QUALITY certification for the…
The Plant Science Student Conference (PSSC) has been organised by students from the two Leibniz institutes, IPK and IPB, every year for the last 20 years. In this interview, Christina Wäsch (IPK) and…
Cheng, L.; Zhang, H.; Cui, H.; Davari, M. D.; Wei, B.; Wang, W.; Yuan, Q.;Efficient enzyme-catalyzed production of diosgenin: inspired by the biotransformation mechanisms of steroid saponins in Talaromyces stollii CLY-6Green Chemistry235896-5910(2021)DOI: 10.1039/d0gc04152a
Diosgenin is an important raw material of numerous synthetic steroidal drugs, such as sex hormones, contraceptives, and cortisone. Diosgenin production by enzymatic catalysis provides a solution for avoiding severe environmental issues caused by conventional acid hydrolysis. However, exploring high-efficiency enzymes and setting up catalytic processes still remain challenging. Herein, we identified a strain named Talaromyces stollii CLY-6, which showed efficient transformation of steroid saponins into diosgenin. Through genomic analysis and protein fingerprinting, two novel steroid saponin glycosidases (Rhase-TS: α-L-rhamnosidase; Gluase-TS: β-D-glucosidase) were discovered from Talaromyces stollii CLY-6. Enzyme over-expression and functional investigation suggested that Rhase-TS is capable of specifically hydrolyzing the terminal α-L-1,2-rhamnoside of steroid saponins, and Gluase-TS can release the residual glucose groups, thereby revealing a microbial transformation mechanism of steroid saponins and providing an enzymatic foundation for guiding diosgenin production. Notably, Rhase-TS exhibited excellent enzymatic properties with high thermostability (<70 °C), broad pH stability (pH 3.0 to 10.0), high rhamnose tolerance (Ki: 0.5 M), and high catalytic activity (136.34 U mg−1). Inspired by the above studies, a whole-enzyme-catalyzed approach was explored and optimized to efficiently prepare diosgenin at the gram-level (up to 96.5% yield). Compared with conventional acid hydrolysis, this enzyme-based approach showed a significant advantage in reducing environmental pollution and increasing economic benefits, offering a promising alternative for green and eco-friendly diosgenin production.
Publications
Adjedje, V. K. B.; Schell, E.; Wolf, Y. L.; Laub, A.; Weissenborn, M. J.; Binder, W. H.;Enzymatic degradation of synthetic polyisoprenes via surfactant-free polymer emulsificationGreen Chemistry239433-9438(2021)DOI: 10.1039/d1gc03515k
We report the enzymatic degradation of a synthetic polyisoprene with a cis : trans ratio of 56 : 27 for the first time. Utilizing a bioinspired surfactant-free emulsification strategy in water resulted in substantially increased enzymatic activities with the latex clearing protein LcpK30.