The chemical properties of alicyclic heterocycles are similar to those of the corresponding chain compounds. Compound: Bis(2,5-dioxopyrrolidin-1-yl) O,O’-ethane-1,2-diyl disuccinate, is researched, Molecular C18H20N2O12, CAS is 70539-42-3, about Cross-linked enzyme aggregates (CLEAs) of Penicillium notatum lipase enzyme with improved activity, stability and reusability characteristics, the main research direction is Penicillium lipase immobilization cross linked enzyme aggregate EGNHS; ethylene glycol bissuccinimidoylsuccinate CLEA lipase thermostability activity; Activity recovery; Cross-linked enzyme aggregates; Lipase; Pencillium notatum; Reusability; Thermo-stability.Computed Properties of C18H20N2O12.
Cross-linked enzyme aggregates (CLEAs) are considered as an effective tool for the immobilization of enzyme. In this study, Pencillium notatum lipase (PNL) was immobilized as carrier free cross-linked enzyme aggregates using glutaraldehyde (GLA) and Ethylene glycol-bis [succinic acid N-hydroxysuccinimide] (EG-NHS) as crosslinking agents. The optimal conditions for the synthesis of an efficient lipase CLEAs such as precipitant type, the nature and amount of crosslinking reagent, and crosslinking time were optimized. The recovered activities of CLEAs were considerably dependent on the concentration of GLA; however, the activity recovery was not severely affected by EG-NHS as a mild cross-linker. The EG-NHS aggregates displayed superior hydrolytic (52.08 ± 2.52%) and esterification (64.42%) activities as compared to GLA aggregates which showed 23.8 ± 1.86 and 34.54% of hydrolytic and esterification activity, resp. Morphol. anal. by fluorescence and scanning electron microscope revealed that EG-NHS aggregates were smaller in size with larger surface area compared to GLA aggregates. The pH optima of both types of CLEAs were displaced to slightly alk. region and higher temperature as compared to native enzyme. Highest enzyme activity of CLEAs was achieved at the pH of 9.0 and 42 °C temperature Moreover, a significant improvement in the thermal resistance was also recorded after immobilization. After ten reusability cycles in aqueous medium, GLA and EG-NHS cross-linked lipase CLEAs preserved 63.62% and 70.9% of their original activities, resp. The results suggest that this novel CLEA-lipase is potentially usable in many industrial applications.
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Reference:
Benzofuran – Wikipedia,
Benzofuran | C8H6O – PubChem