Article

Immobilization of Active Human Carboxylesterase 1 in Biomimetic Silica Nanoparticles

Dept. of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
Biotechnology Progress (Impact Factor: 1.88). 05/2011; 27(3):863-9. DOI: 10.1002/btpr.604
Source: PubMed

ABSTRACT The encapsulation of proteins in biomimetic silica has recently been shown to successfully maintain enzymes in their active state. Organophosphate (OP) compounds are used as pesticides as well as potent chemical warfare nerve agents. Because these toxicants are life threatening, we sought to generate biomimetic silicas capable of responding to OPs. Here, we present the silica encapsulation of human drug metabolism enzyme carboxylesterase 1 (hCE1) in the presence of a range of catalysts. hCE1 was successfully encapsulated into silica particles when lysozyme or the peptide R5 were used as catalysts; in contrast, polyethyleneimine, a catalyst used to encapuslate other enzymes, did not facilitate hCE1 entrapment. hCE1 silica particles in a column chromatography format respond to the presence of the OP pesticides paraoxon and dimethyl-p-nitrophenyl phosphate in solution. These results may lead to novel approaches to detect OP pesticides or other weaponized agents that bind hCE1.

0 Followers
 · 
67 Views
  • Source
    • "Gardimalla et al. (2005) Single-enzyme nanoparticles (SEN) a-Chymotrypsin and trypsin 3.4.21.1 and 3.4.4.4 Kim & Grate (2003) Silica nanosystems a-Amylase and carboxylesterase 3.2.1.1 and 3.1.1.1 Bellino et al. (2010) and Edwards et al. (2011) "
    [Show abstract] [Hide abstract]
    ABSTRACT: Therapeutic enzymes are one of the most promising applications of this century in the field of pharmaceutics. Biocatalyst properties can be improved by enzyme immobilization on nanoobjects, thereby increasing stability and reusability and also enhancing the targeting to specific tissues and cells. Therapeutic biocatalyst–nanodevice complexes will provide new tools for the diagnosis and treatment of old and newly emerging pathologies. Among the advantages of this approach are the wide span and diverse range of possible materials and biocatalysts that promise to make the matrix–enzyme combination a unique modality for therapeutic delivery. This review focuses on the most significant techniques and nanomaterials used for enzyme immobilization such as metallic superparamagnetic, silica, and polymeric and single-enzyme nanoparticles. Finally, a review of the application of these nanodevices to different pathologies and modes of administration is presented. In short, since therapeutic enzymes constitute a highly promising alternative for treating a variety of pathologies more effectively, this review is aimed at providing the comprehensive summary needed to understand and improve this burgeoning area.
    Critical Reviews in Biotechnology 06/2015; DOI:10.3109/07388551.2014.990414 · 7.84 Impact Factor
  • Source
    • "Carboxylesterases enzyme are hydrolyse a wide range of endogenous and exogenous esters (Edwards et al., 2011; Lagas et al., 2012). The main physiological role is often unknown and varies among species but they are believed to be significant in the hydrolytic detoxification of some organophosphorus pesticides and an additional role as alternative sites of organophosphorus binding and phosphorylation (Bruxel et al., 2012; Edwards et al., 2011; Parathath et al., 2011). In general, carboxylesterase activity in sheep revelations greater sensitivity to organophosphorus compounds than other esterases (del Loandos et al., 2012) and its assessable activity is higher (Hatfield et al., 2011; Wang et al., 2011). "
  • Source
    • "Carboxylesterases enzyme are hydrolyse a wide range of endogenous and exogenous esters (Edwards et al., 2011; Lagas et al., 2012). The main physiological role is often unknown and varies among species but they are believed to be significant in the hydrolytic detoxification of some organophosphorus pesticides and an additional role as alternative sites of organophosphorus binding and phosphorylation (Bruxel et al., 2012; Edwards et al., 2011; Parathath et al., 2011). In general, carboxylesterase activity in sheep revelations greater sensitivity to organophosphorus compounds than other esterases (del Loandos et al., 2012) and its assessable activity is higher (Hatfield et al., 2011; Wang et al., 2011). "
    [Show abstract] [Hide abstract]
    ABSTRACT: The purpose of this study was to investigate the freezing correlations between the storage -80 °C and -20 °C. A further aim was to establish a foundation for the applicability of carboxylesterase in sheep as biochemical biomarkers for the evaluation of exposure to organophosphorus pesticides. Carboxylesterase is an enzyme that is capable of hydrolysing a wide variety of carboxylic acid esters. Determination of carboxylesterase in blood contents is the appropriate tool for the diagnosis of organophosphorus exposures. Carboxylesterase were determined by the Clement and Erhardt method, adapted for a plate reader. Biochemical products are prevalent in animals destined for human ingesting in world with serious public health inferences. Animal handlers are at risk of pollution and can serve as source of pollution to susceptible hosts. Targeted pest regulator of poisoned animals, concerted veterinary efforts, professional health instruction, active attachment of animal careers are necessary for effective control. In general, a significant increasing was seen for carboxylesterase activities after 3 weeks at -80 ºC and linear regression of mean carboxylesterase observed in all individual samples on weeks of two freezing for plasma (R 2 = 0819; P < 0.001).
    Journal of Engineering and Applied Science 10/2012; available online(2051-0853):361-365.
Show more