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1.
Exp Eye Res ; 234: 109601, 2023 09.
Article in English | MEDLINE | ID: mdl-37488008

ABSTRACT

Bandage contact lenses have an increased affinity to accumulate tear film proteins and bacteria during wear. Among the wide variety of tear film proteins, lysozyme has attracted the most attention for several reasons, including the fact that it is found at a high concentration in the tear film, has exceptional antibacterial and antibiofilm properties, and its significant deposits onto contact lenses. This study aims to evaluate the effect of lysozyme on bacterial biofilm formation on bandage contact lenses. For this purpose, several methods, including microtiter plate test and Colony Forming Unit (CFU) assay have been used to determine antibacterial and antibiofilm characteristics of lysozyme against the two most frequent contact lens-induced bacterial ocular infections, Staphylococcus aureus, and Pseudomonas aeruginosa. The results of these assays demonstrate lysozyme potential to inhibit 57.9% and 80.7% of the growth of S. aureus and P. aeruginosa, respectively. In addition, biofilm formations of P. aeruginosa and S. aureus reduced by 38.3% and 62.7%, respectively due to the antibiofilm effect of lysozyme. SEM and AFM imaging were utilized to visualize lysozyme antibacterial activity and topography changes of the contact lens surface, respectively, in the presence/absence of lysozyme. The results indicated that lysozyme can efficiently attack both gram-positive and gram-negative bacteria and consequently lysozyme-functionalized bandage contact lenses can reduce the risk of ocular infection after eye surgery.


Subject(s)
Contact Lenses, Hydrophilic , Muramidase , Muramidase/pharmacology , Bacterial Adhesion , Anti-Bacterial Agents/pharmacology , Staphylococcus aureus , Gram-Negative Bacteria/metabolism , Gram-Positive Bacteria/metabolism , Pseudomonas aeruginosa , Biofilms , Bandages
2.
Chemosphere ; 312(Pt 1): 137185, 2023 Jan.
Article in English | MEDLINE | ID: mdl-36368538

ABSTRACT

The global health status is highly affected by the growing pace of urbanization, new lifestyles, climate changes, and resource exploitation. Modern technologies pave a promising way to deal with severe concerns toward sustainable development. Herein, we provided a comprehensive review of some popular biotechnological advancements regarding the progress achieved in water, food, and medicine, as the most substantial fields related to public health. The emergence of novel organic/inorganic materials has brought about significant improvement in conventional water treatment techniques, anti-fouling approaches, anti-microbial agents, food processing, biosensors, drug delivery systems, and implants. Particularly, a growing interest has been devoted to nanomaterials and their application for developing novel structures or improving the characteristics of standard components. Also, bioinspired materials have been widely used to improve the performance, efficiency, accuracy, stability, safety, and cost-effectiveness of traditional systems. On the other side, the fabrication of innovative devices for precisely monitoring and managing various ecosystem and human health issues is of great importance. Above all, exceptional advancements in designing ion-selective electrodes (ISEs), microelectromechanical systems (MEMs), and implantable medical devices have altered the future landscape of environmental and biomedical research. This review paper aimed to shed light on the wide-ranging materials and devices that have been developed for health applications and mainly focused on the impact of nanotechnology in this field.


Subject(s)
Biosensing Techniques , Nanostructures , Humans , Ecosystem , Biosensing Techniques/methods , Nanotechnology , Delivery of Health Care
3.
Crit Rev Food Sci Nutr ; 61(19): 3160-3196, 2021.
Article in English | MEDLINE | ID: mdl-32715740

ABSTRACT

The demand for food and beverage markets has increased as a result of population increase and in view of health awareness. The quality of products from food processing industry has to be improved economically by incorporating greener methodologies that enhances the safety and shelf life via the enzymes application while maintaining the essential nutritional qualities. The utilization of enzymes is rendered more favorable in industrial practices via the modification of their characteristics as attested by studies on enzyme immobilization pertaining to different stages of food and beverage processing; these studies have enhanced the catalytic activity, stability of enzymes and lowered the overall cost. However, the harsh conditions of industrial processes continue to increase the propensity of enzyme destabilization thus shortening their industrial lifespan namely enzyme leaching, recoverability, uncontrollable orientation and the lack of a general procedure. Innovative studies have strived to provide new tools and materials for the development of systems offering new possibilities for industrial applications of enzymes. Herein, an effort has been made to present up-to-date developments on enzyme immobilization and current challenges in the food and beverage industries in terms of enhancing the enzyme stability.


Subject(s)
Enzymes, Immobilized , Food Industry , Enzyme Stability , Enzymes, Immobilized/metabolism , Technology
4.
Int J Biol Macromol ; 163: 402-413, 2020 Nov 15.
Article in English | MEDLINE | ID: mdl-32629057

ABSTRACT

The covalent immobilization of xylanase onto the trichlorotriazine-functionalized polyethylene glycol grafted magnetic nanoparticles was exploited to generate a stabilized xylanase with improved catalytic activity and stability. Several tools were deployed to monitor the synthesis and immobilization processes, the loading capacity of nanocarrier, and the structural/chemical characteristics of the nanobiocatalyst. The optimum immobilization yield of xylanase was 260 mg xylanase/g nanocarrier in 20 mM phosphate buffer, pH 6.5 at 25 °C. A forward shift in optimum pH (6.5 to 7.5) and temperature (60 to 70 °C) of xylanase was observed after immobilization and the performance of immobilized enzyme was improved at high temperatures and pHs as affirmed by enhancement of vmax (2.69 to 6.01 U/mL) and decreases of Ea (14.61 to 13.41 kJ/mol). An increase in Km from 25.51 to 40.42 mg/mL was recorded after immobilization. The obtained results indicated augmented thermal stability of the immobilized xylanase. Notably, it showed good reusability as validated by retention of 50% of its initial activity after nine recycles in enrichment of the pineapple juice clarification after 120 min incubation at 50 °C, pH 4.5. The structural analysis revealed some partial changes in the α-helix and ß-sheet content of the enzyme after several recycles.


Subject(s)
Enzymes, Immobilized , Fruit and Vegetable Juices , Magnetite Nanoparticles/chemistry , Polyethylene Glycols/chemistry , Triazines/chemistry , Xylosidases/chemistry , Enzyme Stability , Enzymes , Kinetics , Spectrum Analysis , Temperature , Thermodynamics
5.
Food Chem ; 325: 126890, 2020 Apr 22.
Article in English | MEDLINE | ID: mdl-32387928

ABSTRACT

Developing an effective strategy to economically exploitation of pectinase, as one of the most widely used enzymes in food industry, is of utmost importance. Herein, pectinase was covalently immobilized onto polyethylene glycol grafted magnetic nanoparticles via trichlorotriazine with high loading efficiency. The generated immobilized pectinase showed enhanced catalytic activity, improved operational stability, and easily reusability. Thermal and pH stabilities studies showed improved performance of immobilized pectinase especially at extreme points. Compared to free enzyme, the noticeably lower Km and higher vmax values of immobilized pectinase demonstrated the enhanced catalytic activity of this enzyme after immobilization. Besides, the immobilized enzyme exhibited excellent reusability and stability by retaining up to 55 and 94% of its initial activity after 10 recycles and 125 days storage at 25 °C, respectively. Moreover, turbidity reduction occurred up to 59% in treated pineapple juice with immobilized pectinase, suggesting applicability of this system in juice and food-processing industries.

6.
J Colloid Interface Sci ; 536: 261-270, 2019 Feb 15.
Article in English | MEDLINE | ID: mdl-30368098

ABSTRACT

In industrial processes, effective degradation of polygalacturonic acid using immobilized pectinase is preferred over free one due to its stability and efficient functional reuses. Pectinase was covalently conjugated to the surface of cyanuric chloride functionalized chitosan encapsulated magnetite nanoparticles. The results obtained of various analytical tools and biochemical studies demonstrated successful synthesis and immobilization processes, high immobilization efficiency and loading capacity. The circular dichroism (CD) results of free and immobilized pectinase revealed the partial decreases in the α-helices and ß-sheets, and marginal increases in the unordered elements contents of pectinase upon the immobilization onto Fe3O4@Ch-CC nanoparticles, along with stability improvement. The immobilized pectinase was retained about 60% of its initial catalytic activity after 13 recycles at optimum conditions (40 °C, pH 4.5). The storage stability of pectinase was increased due to immobilization, after 75 days storage at 4 °C, the free and immobilized enzyme retained 43% and 74% of the initial activity, respectively. The immobilized pectinase showed higher storage stability and better performance at wider ranges of pH and temperature, compared to free pectinase.


Subject(s)
Chitosan/metabolism , Enzymes, Immobilized/metabolism , Magnetite Nanoparticles/chemistry , Nanoparticles/metabolism , Polygalacturonase/metabolism , Triazines/metabolism , Biocatalysis , Chitosan/chemistry , Enzymes, Immobilized/chemistry , Nanoparticles/chemistry , Particle Size , Polygalacturonase/chemistry , Surface Properties , Triazines/chemistry
7.
Methods Enzymol ; 609: 371-403, 2018.
Article in English | MEDLINE | ID: mdl-30244798

ABSTRACT

Enzymes are used as biocatalysts for analytical purposes in diagnostics and preparative purposes in large-scale industrial processes. Despite perfect catalytic properties of enzymes, their industrial applications are limited due to the drawbacks regarding the lack of long-term stability under process conditions. The difficulties associated with recycling have to be resolved before enzyme implementation at industrial scale. Enzyme immobilization, as a novel approach, can improve the half-life, stability, catalytic activity, and reusability of enzymes. Graphene-based nanomaterials, as nanoscaled and thermostable inorganic carriers, are nontoxic materials and selective modulators for enzyme activity. Herein, we have concentrated on strategies for preparing graphene-based nanocomposites for enzyme immobilization. Nanostructures of graphene, hybrid graphene, and their derivatives with adjustable surface chemistry, caused them to be excellent candidates for immobilization of enzymes. For instance, the synthesis and functionalization of Fe3O4-graphene oxide (GO) hybrids were improved recently, in our research group, using cyanuric chloride and polyethylene glycol bis-amine for the immobilization of xylanase and glucoamylase enzymes, via physical and covalent attachments. Decorating GO nanosheets with Fe3O4 nanoparticles has facilitated the reusability of enzymes and increased the surface area for enzyme loading. The use of these hydrophilic crosslinkers may change the microenvironment of the immobilized enzymes that could result in the enhancement of their catalytic activity. As a result of the fascinating properties of graphene-based nanocarriers, with respect to structures that can be oriented and surfaces that can be modified, in our opinion, they offer some important advantages for biotechnological applications, especially in the areas of enzyme immobilization and medicine.


Subject(s)
Biocatalysis , Biotechnology/trends , Enzymes, Immobilized/chemistry , Graphite/chemistry , Hydrophobic and Hydrophilic Interactions , Nanostructures/chemistry , Organic Chemicals , Polyethylene Glycols/chemical synthesis
8.
Biosens Bioelectron ; 118: 66-79, 2018 Oct 30.
Article in English | MEDLINE | ID: mdl-30056302

ABSTRACT

Water pollution and habitat degradation are the cause of increasing water scarcity and decline in aquatic biodiversity. While the freshwater availability has been declining through past decades, water demand has continued to increase particularly in areas with arid and semi-arid climate. Monitoring of pollutants in wastewater effluents are critical to identifying water pollution area for treatment. Conventional detection methods are not effective in tracing multiple harmful components in wastewater due to their variability along different times and sources. Currently, the development of biosensing instruments attracted significant attention because of their high sensitivity, selectivity, reliability, simplicity, low-cost and real-time response. This paper provides a general overview on reported biosensors, which have been applied for the recognition of important organic chemicals, heavy metals, and microorganisms in dark waters. The significance and successes of nanotechnology in the field of biomolecular detection are also reviewed. The commercially available biosensors and their main challenges in wastewater monitoring are finally discussed.


Subject(s)
Environmental Monitoring/methods , Wastewater/chemistry , Metals, Heavy/analysis , Reproducibility of Results , Water Pollutants, Chemical/analysis
9.
Langmuir ; 31(33): 9219-27, 2015 Aug 25.
Article in English | MEDLINE | ID: mdl-26258956

ABSTRACT

Although several strategies are now available for immobilization of enzymes to magnetic nanoparticles for bioapplications, little progresses have been reported on the use of dendritic or hyperbranched polymers for the same purpose. Herein, we demonstrated synthesis of magnetic nanoparticles supported hyperbranched polyglycerol (MNP/HPG) and a derivative conjugated with citric acid (MNP/HPG-CA) as unique and convenient nanoplatforms for immobilization of enzymes. Then, an important industrial enzyme, xylanase, was immobilized on the nanocarriers to produce robust biocatalysts. A variety of analytical tools were used to study the morphological, structural, and chemical properties of the biocatalysts. Additionally, the results of biocatalyst systems exhibited the substantial improvement of reactivity, reusability, and stability of xylanase due to this strategy, which might confer them a wider range of applications.


Subject(s)
Ascomycota/enzymology , Endo-1,4-beta Xylanases/chemistry , Enzymes, Immobilized/chemistry , Fungal Proteins/chemistry , Nanoparticles/chemistry , Polyethylene Glycols/chemistry , Catalysis , Magnetic Fields
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