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1.
Bioprocess Biosyst Eng ; 44(2): 369-378, 2021 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-32997184

RESUMO

The present study aimed to analyze reaction kinetics and mechanism for the synthesis of propyl benzoate in solvent-free conditions. Lipase was immobilized on Hydroxypropyl methylcellulose (HPMC) and polyvinyl alcohol (PVA) polymer blend by entrapment method. Among different lipases immobilized on a support, Candida cylindracea (CCL) showed excellent activity. Systematic studies were done to optimize the reaction conditions. The activation energy was found to be 16.2 kcal/mol for immobilized CCL. Kinetic parameters were calculated, which depicted that propyl benzoate synthesized using immobilized CCL followed the ternary complex model in which propanol inhibits lipase activity at higher concentrations. Recyclability of the catalyst was checked up to four catalytic cycles and 40% retention of activity was observed up to the fourth cycle. Finally, the applicability of developed protocol to synthesize various alkyl benzoates was explored.


Assuntos
Proteínas de Bactérias/química , Benzoatos/síntese química , Burkholderia cepacia/enzimologia , Candida/enzimologia , Enzimas Imobilizadas/química , Proteínas Fúngicas/química , Lipase/química , Rhizopus oryzae/enzimologia , Biocatálise , Esterificação
2.
Colloids Surf B Biointerfaces ; 130: 84-92, 2015 Jun 01.
Artigo em Inglês | MEDLINE | ID: mdl-25909183

RESUMO

Recombinant expression of Capsicum annuum proteinase inhibitors (CanPI-13) and its application via synthetic carrier for the crop protection is the prime objective of our study. Herein, we explored proteinase inhibitor peptide immobilization on silica based nanospheres and rods followed by its pH mediated release in vitro and in vivo. Initial studies suggested silica nanospheres to be a suitable candidate for peptide immobilization. Furthermore, the interactions were characterized biophysically to ascertain their conformational stability and biological activity. Interestingly, bioactive peptide loading at acidic pH on nanospheres was found to be 62% and showed 56% of peptide release at pH 10, simulating gut milieu of the target pest Helicoverpa armigera. Additionally, in vivo study demonstrated significant reduction in insect body mass (158 mg) as compared to the control insects (265 mg) on 8th day after feeding with CanPI-13 based silica nanospheres. The study confirms that peptide immobilized silica nanosphere is capable of affecting overall growth and development of the feeding insects, which is known to hamper fecundity and fertility of the insects. Our study illustrates the utility and development of peptide-nanocarrier based platform in delivering diverse biologically active complexes specific to gut pH of H. armigera.


Assuntos
Sistemas de Liberação de Medicamentos/métodos , Glicoproteínas/administração & dosagem , Nanosferas/química , Proteínas de Plantas/administração & dosagem , Dióxido de Silício/química , Sequência de Aminoácidos , Animais , Fenômenos Biofísicos , Sistema Digestório/metabolismo , Glicoproteínas/química , Glicoproteínas/metabolismo , Concentração de Íons de Hidrogênio , Proteínas Imobilizadas/administração & dosagem , Proteínas Imobilizadas/química , Proteínas Imobilizadas/metabolismo , Cinética , Microscopia Eletrônica de Varredura , Microscopia Eletrônica de Transmissão , Dados de Sequência Molecular , Mariposas/metabolismo , Nanosferas/ultraestrutura , Proteínas de Plantas/química , Proteínas de Plantas/metabolismo , Homologia de Sequência de Aminoácidos
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