Designing and Formulation of Nanocarriers for "Alzheimer's and Parkinson's" Early Detection and Therapy.

The potential of nanotechnology in advancing the diagnosis and treatment of neurodegenerative diseases is explored in this comprehensive literature review. Through an examination of various studies that utilize nanotechnology models. The aim of this paper is to evaluate whether these models can be considered a significant breakthrough in the field of neurodegeneration. The findings of these studies suggest that nanotechnology has the capacity to improve existing therapeutic approaches, create novel and safe compounds, and develop more precise imaging techniques and diagnostic methods for neurodegenerative diseases. With the emergence of the nanomedicine era, a new and innovative approach to diagnosing and treating these conditions has been introduced. Notably, the researchers' development of a nanocarrier drug delivery tool demonstrates immense potential compared to conventional therapy, as it maximizes therapeutic efficacy and minimizes undesirable side effects.

Stabilization of ß-Galactosidase on Modified Gold Nanoparticles: A Preliminary Biochemical Study to Obtain Lactose-Free Dairy Products for Lactose-Intolerant Individuals.

The unique chemical, optical, and electrical characteristics of nanoparticles make their utilization highly successful in every field of biological sciences as compared to their bulk counterpart. These properties arise as a result of their miniature size, which provides them an excellent surface area-to-volume ratio, inner structure, and shape, and hence increases their surface characteristics. Therefore, this study was undertaken to engineer gold nanoparticles (AuNPs) for improving their catalytic activity and stability in biotechnological processes. The characterization of AuNPs was performed by XRD, UV spectra, and TEM. The synthesized AuNPs were surface-modified by polyvinyl alcohol (PVA) for binding the enzyme in excellent yield. The developed immobilized enzyme system (PVA-AuNPs-ß-galactosidase) displayed pH optima at pH 7.0 and temperature optima at 40 °C. Moreover, the stability of PVA-AuNPs-ß-galactosidase was significantly enhanced at wider pH and temperature ranges and at higher galactose concentrations, in contrast to the free enzyme. ß-galactosidase bound to PVA-modified AuNPs exhibited greater operational activity, even after its sixth reuse. The developed nanosystem may prove useful in producing lactose-free dairy products for lactose-intolerant patients.

Current opinion in Alzheimer's disease therapy by nanotechnology-based approaches.

PURPOSE OF REVIEW: Nanotechnology typically deals with the measuring and modeling of matter at nanometer scale by incorporating the fields of engineering and technology. The most prominent feature of these engineered materials involves their manipulation/modification for imparting new functional properties. The current review covers the most recent findings of Alzheimer's disease (AD) therapeutics based on nanoscience and technology. RECENT FINDINGS: Current studies involve the application of nanotechnology in developing novel diagnostic and therapeutic tools for neurological disorders. Nanotechnology-based approaches can be exploited for limiting/reversing these diseases for promoting functional regeneration of damaged neurons. These strategies offer neuroprotection by facilitating the delivery of drugs and small molecules more effectively across the blood-brain barrier. SUMMARY: Nanotechnology based approaches show promise in improving AD therapeutics. Further replication work on synthesis and surface modification of nanoparticles, longer-term clinical trials, and attempts to increase their impact in treating AD are required.

Role of Glutaraldehyde in Imparting Stability to Immobilized β-Galactosidase Systems

ABSTRACT This review article highlights the role of glutaraldehyde as a matrix activator/stabilizer in imparting higher operational and thermal stability to β-galactosidase (βG) for biotechnological applications. Glutaraldehyde has been used extensively as a crosslinking agent as well as for functionalization of matrices to immobilize β-galactosidase. Immobilized β-galactosidase systems (IβGS) obtained as a result of glutaraldehyde treatment has been employed to hydrolyze whey and milk lactose in batch reactors, continuous packed-bed and fluidized bed reactors under various operational conditions. Moreover, these IβGS have also been utilized for the production of galactooligosaccharides in food, dairy and fermentation industries. It was observed that glutaraldehyde provided remarkable stability to immobilize βG against various physical/chemical denaturants, thus enhancing thermal/operational stability and rendering it more suitable for repeated utilization in industrial scale operations.

In vitro assessment of pharmaceutical potential of ethosomes entrapped with terbinafine hydrochloride.

The present study investigates the entrapment of terbinafine hydrochloride (TH) in ethosomal vesicles via unsonicated and sonication method. Carbopol 934P was incorporated in the best formulation, F6, obtained by sonication method. The formulated ethosomal gel obtained as such i.e. F6(∗) was exploited to achieve a zero order release profile of TH. The composition includes phospholipid, ethanol and propylene glycol. Drug entrapment efficiency (DEE), in-vitro and ex-vivo drug diffusion studies, FT-IR and stability studies of the prepared ethosomes were investigated. The size and shape of F6 ethosomes vesicles were characterized by SEM. In-vitro drug release studies were performed using sigma dialysis membrane in phosphate buffer, pH 7.4 for 12 h while drug content was determined by HPLC. DEE was ranked from 55.33 ± 1.32% to 69.11 ± 2.11%. Highest DEE was seen with F6 ethosomal formulation with a vesicle size of 248 ± 1.02 nm. FT-IR studies confirmed that there was no chemical interaction between drug and excipients used in the formulation. Ex-vivo result suggested that drug diffusion observed after 12 h from F6(∗) and marketed cream (MR) formulations was 74.01 ± 0.62% and 61.45 ± 0.86%, respectively. The results of similarity factor (f 2 values) for MR and F6(∗) ethosomal gel were 85.14 and 42.63, respectively. It revealed that F6(∗) showed dissimilar dissolution profiles. Transdermal flux value for F6(∗) and MR was found to be 144.61 ± 1.28 µg/cm(2)/h and 121.6 ± 1.16 µg/cm(2)/h, respectively. This study disclosed that F6(∗) resides at targeted site for a relatively longer period of time thereby signifying the improved patient compliance.

Elucidating the binding efficacy of ß-galactosidase on graphene by docking approach and its potential application in galacto-oligosaccharide production.

Herein, we propose the synthesis and characterization of graphene for the immobilization of ß-galactosidase for improved galacto-oligosaccharide (GOS) production. The size of synthesized graphene was observed to be 25 nm by TEM analysis while interaction of enzyme with the nanosupport was observed by FTIR spectroscopy. Docking was obtained using molecular docking program Dock v.6.5 while the visual analyses and illustration of protein-ligand complex were investigated by utilizing chimera v.1.6.2 and PyMOL v.1.3 softwares. Immobilized ß-galactosidase (IßG) showed improved stability against various physical and chemical denaturants. Km of IßG was increased to 6.41 mM as compared to 2.38 mM of soluble enzyme without bringing significant change in Vmax value. Maximum GOS content also registered an increase in lactose conversion. The maximum GOS production was achieved by immobilized enzyme at specific temperature and time. Hence, the developed nanosupport can be further exploited for developing a biosensor involving ß-galactosidase or for immobilization of other industrially/therapeutically important enzymes.

Role of Nanodiamonds in Drug Delivery and Stem Cell Therapy.

CONTEXT: The use of nanotechnology in medicine and more specifically drug delivery is set to spread rapidly. Currently many substances are under investigation for drug delivery and more specifically for cancer therapy. EVIDENCE ACQUISITION: Nanodiamonds (NDs) have contributed significantly in the development of highly efficient and successful drug delivery systems, and in stem cell therapy. Drug delivery through NDs is an intricate and complex process that deserves special attention to unravel underlying molecular mechanisms in order to overcome certain bottlenecks associated with it. It has already been established that NDs based drug delivery systems have excellent biocompatibility, nontoxicity, photostability and facile surface functionalization properties. RESULTS: There is mounting evidence that suggests that such conjugated delivery systems well retain the properties of nanoparticles like small size, large surface area to volume ratio that provide greater biocatalytic activity to the attached drug in terms of selectivity, loading and stability. CONCLUSIONS: NDs based drug delivery systems may form the basis for the development of effective novel drug delivery vehicles with salient features that may facilitate their utility in fluorescence imaging, target specificity and sustainedrelease.

Immobilization of Aspergillus oryzae ß-Galactosidase on Cellulose Acetate-Polymethylmethacrylate Membrane and Its Application in Hydrolysis of Lactose from Milk and Whey.

The present study demonstrates the immobilization of Aspergillus oryzae ß-galactosidase on cellulose acetate-polymethylmethacrylate (CA-PMMA) membrane and its application in hydrolyzing lactose in dairy industries. The effect of physical and chemical denaturants like pH, temperature, product inhibition by galactose, storage stability, and reuse number of the enzyme immobilized on CA-PMMA membrane has been investigated. Lactose was hydrolyzed from milk and whey in batch reactors at 50°C by free and immobilized ß-galactosidase (IßG). Optimum pH for the free and immobilized enzyme was found to be the same, that is, 4.5. However, IßG retained greater fractions of catalytic activity at lower and higher pH ranges. The temperature optimum for the immobilized enzyme was increased by 10°C. Moreover, Michaelis-Menten constant was increased for IßG as compared to the native one while maximum reaction rate was reduced for the immobilized enzyme. The preserved activity of free and immobilized enzyme was found to be 45% and 83%, respectively, after five weeks of storage at 4°C. Reusability of IßG was observed to be 86% even after fifth repeated use, thereby signifying its application in lactose hydrolysis (as shown in lab-scale batch reactors) in various dairy products including milk and whey.

Catalyzed degradation of disperse dyes by calcium alginate-pectin entrapped bitter gourd (Momordica charantia) peroxidase.

Calcium-alginate pectin entrapped bitter gourd peroxidase (BGP) has been employed for the treatment of disperse dyes: Disperse Brown 1 (DB 1) and Disperse Red 17 (DR 17). Peroxidase alone was unable to decolorize DR 17 and DB 1. However, the investigated dyes were decolorized maximally by BGP in the presence of 0.2 mmol/L redox mediator, violuric acid (VA). A slow decrease in percent decolorization was observed when VA concentration was higher than 0.2 mmol/L which could likely be due to the high reactivity of its aminoxyl radical (> N-O*) intermediate, that might undergo chemical reactions with aromatic amino acid side chains of the enzyme thereby inactivating it. Maximum decolorization of the dyes was observed at pH 3.0 and 40 degrees C within 2 hr of incubation. Immobilized peroxidase decolorized 98% DR 17 and 71% DB 1 using 35 U of BGP in batch process in 90 min. Immobilized enzyme decolorized 85% DR 17 and 51% DB 1 whereas soluble enzyme decolorized DR 17 to 48% and DB 1 to 30% at 60 degrees C. UV-visible spectral analysis was used to evaluate the degradation of these dyes and their toxicity was tested by Allium cepa test. The generally observed higher stability of the bioaffinity bound enzymes against various forms of inactivation may be related to the specific and strong binding of enzyme with bioaffinity support which prevents the unfolding/denaturation of enzyme. Thus entrapped peroxidase was found to be effective in the decolorization of the investigated dyes.

Adsorption of peroxidase on Celite 545 directly from ammonium sulfate fractionated white radish (Raphanus sativus) proteins.

This paper demonstrates the direct immobilization of peroxidase from ammonium sulfate fractionated white radish proteins on an inorganic support, Celite 545. The adsorbed peroxidase was crosslinked by using glutaraldehyde. The activity yield for white radish peroxidase was adsorbed on Celite 545 was 70% and this activity was decreased and remained 60% of the initial activity after crosslinking by glutaraldehyde. The pH and temperature-optima for both soluble and immobilized peroxidase was at pH 5.5 and 40 degrees C. Immobilized peroxidase retained higher stability against heat and water-miscible organic solvents. In the presence of 5.0 mM mercuric chloride, immobilized white radish peroxidase retained 41% of its initial activity while the free enzyme lost 93% activity. Soluble enzyme lost 61% of its initial activity while immobilized peroxidase retained 86% of the original activity when exposed to 0.02 mM sodium azide for 1 h. The K(m) values were 0.056 and 0.07 mM for free and immobilized enzyme, respectively. Immobilized white radish peroxidase exhibited lower V(max) as compared to the soluble enzyme. Immobilized peroxidase preparation showed better storage stability as compared to its soluble counterpart.

Application of calcium alginate-starch entrapped bitter gourd (Momordica charantia) peroxidase for the removal of colored compounds from a textile effluent in batch as well as in continuous reactor.

Calcium alginate-starch entrapped bitter gourd peroxidase has been employed for the treatment of a textile industrial effluent in batch as well as in continuous reactor. The textile effluent was recalcitrant to decolorization by bitter gourd peroxidase; thus, its decolorization was examined in the presence of a redox mediator, 1.0 mM 1-hydroxybenzotriazole. Immobilized enzyme exhibited same pH and temperature optima for effluent decolorization as attained by soluble enzyme. Immobilized enzyme could effectively remove more than 70% of effluent color in a stirred batch process after 3 h of incubation. Entrapped bitter gourd peroxidase retained 59% effluent decolorization reusability even after its tenth repeated use. The two-reactor system containing calcium alginate-starch entrapped enzyme retained more than 50% textile effluent decolorization efficiency even after 2 months of its operation. The absorption spectra of the treated effluent exhibited a marked difference in the absorption at various wavelengths as compared to untreated effluent. The use of a two-reactor system containing immobilized enzyme and an adsorbent will be significantly successful for treating industrial effluents at large scale, and it will help in getting water free from aromatic pollutants.

Phenol-mediated decolorization and removal of disperse dyes by bitter gourd (Momordica charantia) peroxidase.

Salt-fractionated bitter gourd (Momordica charantia) proteins were employed for the decolorization of disperse dyes in the presence of H2O2. The effect of various experimental conditions such as concentration of enzyme, H2O2, phenol, reaction time, pH and temperature on the decolorization of dyes was investigated. Dyes were recalcitrant to the decolorization catalysed by bitter gourd peroxidase. However, these dyes were decolorized significantly in the presence of a redox mediator, phenol. Bitter gourd peroxidase (0.215 U/mL) could decolorize about 60% of Disperse Red 17 in the presence of 0.2 mM phenol, whereas Disperse Brown 1 was decolorized by only 40% even in the presence of 0.4 mM phenol. Maximum decolorization of dyes was achieved in the presence of 0.75 mM H2O2 in a buffer ofpH 3.0 and 40 degrees C within 30 min. The K(m) values obtained were 0.625 mg/(L x h) and 2.5 mg/(L x h) for Disperse Red 17 and Disperse Brown 1, respectively. In all the experiments, Disperse Brown 1 was found to be more recalcitrant to decolorization catalysed by bitter gourd peroxidise, as compared to Disperse Red 17.