Development of novel delivery system for nanoencapsulation of catalase: formulation, characterization, and in vivo evaluation using oxidative skin injury model

Abstract

One of the main challenges for successful pharmaceutical application of Catalase (CAT) is maintaining its stability. Physical immobilization of CAT through nano-encapsulation was proposed to resolve this challenge. CAT encapsulating niosomes (e-CAT) were prepared using Brij 30, 52, 76, 92, and 97 in the presence of cholesterol (Ch) by thin film hydration method. Niosomes were characterized for encapsulation efficiency % (EE), size, poly-dispersity index (PI), and morphology. Kinetic parameters, pH optimum, thermal stability, and reusability of CAT were determined. The influence of optimized e-CAT dispersion onto thermally injured rat skin was evaluated. Results revealed that encapsulation enhanced CAT catalytic efficiency (V/K). Free CAT and e-CAT had pH optimum at 7.0. e-CAT exhibited improved thermal stability where it retained 50% residual activity at 60 °C. Free CAT lost its activity after three consecutive operational cycles; however, e-CAT retained 60% of its initial activity following 12 cycles. After 24 h of topical application on thermal injury, a significant difference in lesion size was observed with e-CAT compared with the control group. Based on these encouraging results, CAT immobilization demonstrated a promising novel delivery system that enhances its operational stability. In addition, nano-encapsulated CAT can be anticipated to be beneficial in skin oxidative injury.

Platelet-Rich Fibrin Can Neutralize Hydrogen Peroxide-Induced Cell Death in Gingival Fibroblasts

“…Catalase might be involved in explaining the positive effects of PRF in refractory skin ulcers [6]. For example, the local application of catalase on thermal skin injury helped to reduce the lesion size in rats [39]. The present data are also relevant to consider heating when preparing an injectable PRF mixture consisting of autologous albumin gel and liquid platelet-rich fibrin.…”

Cubic Liquid Crystalline Nanostructures Involving Catalase and Curcumin: BioSAXS Study and Catalase Peroxidatic Function after Cubosomal Nanoparticle Treatment of Differentiated SH-SY5Y Cells

“…Thus, catalase exhibits a short half-life and poor operational stability and reusability as an enzyme, which limits its potential therapeutic applications [55,56,57,58,59,60]. The unstable biomacromolecule can be immobilized in order to increase its stability and improve its enzymatic performance, solubility and specificity [61,62,63,64,65,66,67]. Catalase has been immobilized on solid supports from natural polymers (chitosan, gelatin, etc.…”

“…), and inorganic particles (calcium carbonate, silica, gold, etc.) [61,62,63,64,65,66,67]. This helped to overcome the enzyme’s degradation or deactivation.…”

Bio-inspired trypsin-chitosan cross-linked enzyme aggregates: a versatile approach for stabilization through carrier-free immobilization

“…The reason for observed loss in enzymatic activity could be due to subjecting the trypsin enzyme to mechanical stress during consecutive centrifugation cycles which might have caused conformational and morphological changes (Dalal et al, 2007;Mahmod et al, 2016). An observed enhancement of enzyme re-usability was reported earlier for different enzymes using various immobilization techniques such as catalase (Abdel-Mageed et al, 2018), α-amylase (Talekar et al, 2012;Abdel-Mageed et al, 2019), and trypsin (Sun et al, 2013;Mahmod et al, 2016).…”