Immobilized enzymatic catalysts are widely used in the chemical and pharmaceutical industries. As Candida antarctica lipase B (CALB) is one of the more commonly used biocatalysts, we attempted to design an optimal lipase-catalytic system. In order to do that, we investigated the enantioselectivity and lipolytic activity of CALB immobilized on 12 different supports. Immobilization of lipase on IB-D152 allowed us to achieve hyperactivation (178%) in lipolytic activity tests. Moreover, the conversion in enantioselective esterification increased 43-fold, when proceeding with lipase-immobilized on IB-S861. The immobilized form exhibited a constant high catalytic activity in the temperature range of 25 to 55°C. Additionally, the lipase immobilized on IB-D152 exhibited a higher lipolytic activity in the pH range of 6 to 9 compared with the native form. Interestingly, our investigations showed that IB-S500 and IB-S60S offered a possibility of application in catalysis in both organic and aqueous solvents. A significant link between the reaction media, the substrates, the supports and the lipase was confirmed. In our enzymatic investigations, high-performance liquid chromatography (HPLC) and the titrimetric method, as well as the Bradford method were employed.
Background: Many OTC drugs are available in non-pharmacy outlets, and as such the risk of overuse and/or improper use of this class of drugs is more likely. In light of this observation, our study was conducted with the aim of exploring opinions on non-pharmaceutical distribution among Polish patients. This study was a part of an informative project to educate patients about the possible risks associated with the use of OTC medicines. Methods: We conducted a cross-sectional study among Polish patients in which we used an authorial questionnaire, previously tested via content, face validity, and a pilot study. The questionnaire was distributed both electronically and in a traditional form. Results: ‘Time saving’ had a statistically significant role in the patient’s decision about purchasing drugs in a non-pharmacy outlet (p = 0.0052; R = 0.276994). The lack of a pharmacist’s consultation/advice (p = 0.0072; R = −0.3290490), improper storage (p = 0.0044; R = −0.238246), risk of overdose (p = 0.0125; R = −0.189564), and the risk of purchasing out-of-date drugs (p = 0.0125; R = −0.145411), as well as the risk of purchasing falsified drugs (p = 0.0265; R = −0.159428), were all associated with the patient’s non-willingness to purchase drugs in non-pharmacy outlets. Patients supported the idea of the elimination of non-pharmacy outlet distribution (p = 0.0074; R = −0.195932); they also emphasized that they are advocates of purchasing drugs only in community pharmacies (p = 0.0006; R = −0.238625). Conclusion: Patients are aware of the risks associated with buying drugs outside of community pharmacies. They perceived pharmacists as professional health care advisors and supported the fact that OTC drugs should be available only via pharmaceutical distribution.
Lipases are commonly applied in the pharmaceutical and chemical industry, especially in immobilized form. The use of immobilized lipases facilitates the design of reactors and control of reactions, for example, fast stopping the reaction. The immobilization procedure should increase the stability of the lipase and its activity, as well as be simple and efficient. Lipase B from Candida antarctica (CAL-B) is an enzyme from the lipase group, isolated from the Candida antarctica species. CAL-B has the highest activity in non-polar organic solvents, such as hexane and toluene, and the lowest in polar solvents, e.g. acetonitrile. Due to its hydrolytic properties, this enzyme degrades triglycerides of fatty acids to free fatty acids (FFA) and glycerol. Described lipase is often immobilized, in the aim to increase enantioselective and lipolytic activity. The kinetic and dynamic resolution with the application of lipase is one of the ways in obtaining an enantiopure form of the drugs, which usually are more effective and safer for the patient. The CAL-B could be also applied in the kinetic resolution of compounds being building blocks, derivates of drugs or conjugated forms. Furthermore, the CAL-B is used in the reactions in receiving of organic compounds, which are the natural origin, especially vegetable. Based on the presented data, it can be concluded, that CAL-B is an enzyme with a wide application in the biosynthesis of compounds with therapeutic activity.
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