scholarly journals Is Laccase Enzyme an Answer for Sustainable Thatch Management in Turfgrass Systems: A Review

2019 ◽  
Vol 19 (1) ◽  
Author(s):  
Sudeep Singh Sidhu
Keyword(s):  
Laccase Enzyme

The Use of Ultrasound in Bio-Treatment of Jute Yarn with Laccase Enzyme

2019 ◽  
Vol 12 (4) ◽  
pp. 275-286
Author(s):  
Ali A. Zolriasatein
Keyword(s):  
Tensile Strength ◽  
Reaction Times ◽  
Complete Removal ◽  
Jute Fiber ◽  
Light Fastness ◽  
Color Strength ◽  
Yellowness Index ◽  
Laccase Enzyme ◽  
Enzymatic Delignification ◽  
Jute Yarn

Background and Objective: Jute fiber is highly sensitive to the action of light. Significant features of the photochemical changes lose its tensile strength and develop a yellow color. It has been proved that the phenolic structure of lignin is responsible for the yellowing of jute fiber. In order to remove lignin, jute yarns were treated with laccase enzyme in different treatment times and ultrasonic powers. Lower whiteness index and higher yellowness index values were obtained by the laccase-ultrasound system in contrast to conventional laccase treatment. Methods: The laccase enzyme which entered the fibers by applying ultrasound, decreased the tensile strength while the loss in tensile strength was lower at high ultrasound intensities. FT-IR spectrum showed that the band at 1634 cm-1 assigned to lignin completely disappeared after laccase treatment in the presence of ultrasound. The absence of this peak in the laccase-ultrasound treated jute yarn suggests complete removal of lignin. Change in the morphology of fibers was observed by SEM before and after enzymatic delignification. The laccase-ultrasound treated yarns showed a rougher surface and more porosity. On the other hand, it was more effective in fibrillation of the jute fibers than the conventional method. Finally, bio-treated jute yarns were dyed with basic and reactive dyes. Results: The results indicated that at low intensities of ultrasound and relatively long reaction times, lignin can be more effectively removed and dye strength (K/S) increased to a higher extent. Laccase-ultrasound treatment increased the color strength by 33.65% and 23.40% for reactive and basic dyes respectively. Conclusion: In the case of light fastness, the conventional laccase treated yarns provided better protection than laccase-ultrasound treated yarns.

scholarly journals Partial purification and biochemical characterization of a new highly acidic NYSO laccase from Alcaligenes faecalis

2020 ◽  
Vol 18 (1) ◽  
Author(s):  
Soad A. Abdelgalil ◽  
Ahmad R. Attia ◽  
Reyed M. Reyed ◽  
Nadia A. Soliman
Keyword(s):  
Enzyme Activity ◽  
Sodium Dodecyl ◽  
Alcaligenes Faecalis ◽  
Maximum Activity ◽  
Sodium Oxalate ◽  
Partial Purification ◽  
Bromophenol Blue ◽  
Bromocresol Purple ◽  
Laccase Enzyme

Abstract Background Due to the multitude industrial applications of ligninolytic enzymes, their demands are increasing. Partial purification and intensive characterization of contemporary highly acidic laccase enzyme produced by an Egyptian local isolate designated Alcaligenes faecalis NYSO were studied in the present investigation. Results Alcaligenes faecalis NYSO laccase has been partially purified and intensively biochemically characterized. It was noticed that 40–60% ammonium sulfate saturation showed maximum activity. A protein band with an apparent molecular mass of ~ 50 kDa related to NYSO laccase was identified through SDS-PAGE and zymography. The partially purified enzyme exhibited maximum activity at 55 °C and pH suboptimal (2.5–5.0). Remarkable activation for enzyme activity was recognized after 10-min exposure to temperatures (T) 50, 60, and 70 °C; time elongation caused inactivation, where ~ 50% of activity was lost after a 7-h exposure to 60 °C. Some metal ions Cu2+, Zn2+, Co2+, Ni2+, Mn2+, Cd2+, Cr2+, and Mg2+ caused strong stimulation for enzyme activity, but Fe2+ and Hg2+ reduced the activity. One millimolar of chelating agents [ethylenediamine tetraacetic acid (EDTA), sodium citrate, and sodium oxalate] caused strong activation for enzyme activity. Sodium dodecyl sulfate (SDS), cysteine-HCl, dithiothreitol (DTT), β-mercaptoethanol, thioglycolic acid, and sodium azide caused strong inhibition for NYSO laccase activity even at low concentration. One millimolar of urea, imidazole, kojic acid, phenylmethylsulfonyl fluoride (PMSF), H2O2, and Triton X-100 caused activation. The partially purified NYSO laccase had decolorization activity towards different dyes such as congo red, crystal violet, methylene blue, fast green, basic fuchsin, bromophenol blue, malachite green, bromocresol purple eriochrome black T, and Coomassie Brilliant Blue R-250 with various degree of degradation. Also, it had a vast range of substrate specificity including lignin, but with high affinity towards p-anisidine. Conclusion The promising properties of the newly studied laccase enzyme from Alcaligenes faecalis NYSO strain would support several industries such as textile, food, and paper and open the possibility for commercial use in water treatment. It will also open the door to new applications due to its ligninolytic properties in the near future.

Laccase-catalyzed enzymatic dyeing of cotton fabrics

2021 ◽  
pp. 004051752110069
Author(s):  
Rıza Atav ◽  
Bürhan Buğdaycı ◽  
Ömer Bozkurt ◽  
Aylin Yıldız ◽  
Elçin Güneş ◽  
...  
Keyword(s):  
Experimental Studies ◽  
Uv Protection ◽  
Infrared Analysis ◽  
Synthetic Dyes ◽  
Protection Factor ◽  
Knitted Fabrics ◽  
Reactive Dyeing ◽  
Dyeing Process ◽  
Laccase Enzyme ◽  
Color Reproducibility

As some synthetic dyes are regarded to be toxic, mutagenic and carcinogenic, the search for eco-friendly alternatives for the synthesis of dyes and coloration has gained importance. For this reason, this study focused on finding new eco-friendly alternatives for coloring cotton. 100% cotton knitted fabrics were subjected to enzymatic coloration using a commercial laccase enzyme and various precursors. After determining the colors, the effect of pH on the enzymatic dyeing process was investigated. Then the optimization of reaction conditions was also realized statistically for the precursors giving the best results in terms of color. With the aim of obtaining further improvements in color-yield values obtained in enzymatic dyeings, the effect of the pretreatment process and the use of ultrasound were also investigated. Furthermore, the reaction pathways in enzymatic coloration were explained and results were confirmed by means of Fourier Transformed Infrared analysis. As a result of experimental studies, red and lilac colors could be successfully obtained on cotton for the first time in the literature. In this way, the theoretical basis of enzymatic dye synthesis and dyeing of cotton was clarified comprehensively. Furthermore, technical (color reproducibility; washing, rubbing, light and perspiration-fastness values; and UV protection factor), economical (chemical, energy and water consumption required for dyeing (including aftertreatments) of 1 kg fabric) and ecological aspects of enzymatic dyeings were compared with reactive dyeing. According to the experimental results it was found that biological treatment alone was enough for wastewater of enzymatic coloring, while chemical treatment will also be needed in reactive dyeing wastewater. Furthermore, color reproducibility, evenness and UV protection properties of dyed samples were comparable with that of reactive dyeings. However, in terms of the fastness levels achieved, the enzymatic coloring was far behind the reactive dyeing.

Laccase Enzyme in Nanotechnology and their Environmental Applications

2021 ◽  
Vol 8 (2) ◽  
pp. 2210
Author(s):  
P. Srinivasan ◽  
P. Thiyagarajan ◽  
R. Yuvarajan ◽  
T. Selvankumar
Keyword(s):  
Environmental Applications ◽  
Laccase Enzyme

scholarly journals Bio Efficacy Assay of Laccase isolated and Characterized from Trichoderma viride in Biodegradation of Low Density Polyethylene (LDPE) and Textile Industrial Effluent Dyes

2021 ◽  
Author(s):  
D. Alwin Johnnie ◽  
Reya Issac ◽  
M. Lakshmi Prabha
Keyword(s):  
Trichoderma Viride ◽  
Industrial Effluent ◽  
Low Density Polyethylene ◽  
Textile Dye ◽  
Low Density ◽  
Health Issues ◽  
Environment And Health ◽  
Textile Manufacture ◽  
Living Organisms ◽  
Laccase Enzyme

This study is based on the biosynthesis of laccase enzyme from fungi Trichoderma viride and its exploitation in biodegradation of polyethylene using Laccase mediator system (LMS -Laccase + 1-HBT) in Low Density Polyethylene (LDPE) and in biodegradation of textile industrial effluent dyes. In different parts of our lifespan we have seen the numerous types of plastics are getting degraded by various methods, still the average time to completely degrade a plastic bottle is at least 450 years.Similarly industry produces over 3.6 thousand individual textile dyes today and utilizes more than 8000 toxic chemicals in numerous methods for textile manufacture comprising dyeing and printing. As polyethylene and textile industrial effluent dyes are causing severe hazardous effect on environment and health issues in all kind of living organisms, it is necessary to degrade plastics and textile industrial effluent dyes in rapid way. Recently researchers have come up with an idea of degrading plastic and textile industrial effluent dyes with the help of microorganisms and enzymes much faster than normal rate. The Laccase enzyme extracted was tested for its optimum temperature and pH. Lowry’s method is used for protein estimation. A control and sample LDPE was subjected to LMS. The tensile strength and elongation of the sample was less than that of the control after 5 days of treatment. This study showed that laccase together with 1-HBT helps to biodegrade polyethylene. The purified laccase enzyme was used for the pretreatment assay and post treatment assay. The Laccase degrades certain reactive dyes like Congo red, Acid Red, Methylene Blue, Brilliant Blue, Metallic Blue and Black. Thus recommends the application of laccase in textile dye colour removal (bioremediation).

scholarly journals Short Communication: The higher laccase enzyme producer, Cerrena sp. BMd.TA.1, isolated from Gunung Rinjani National Park, West Nusa Tenggara, Indonesia

2020 ◽  
Vol 21 (8) ◽  
Author(s):  
SARAH ASIH FAULINA ◽  
ASEP HIDAYAT ◽  
SYAMSUL FALAH ◽  
Apri Heri Iswanto
Keyword(s):  
Manganese Peroxidase ◽  
National Park ◽  
Short Communication ◽  
Industrial Effluent ◽  
Fungal Enzymes ◽  
Fungal Laccase ◽  
Synthetic Dye ◽  
Environmental Friendly ◽  
Laccase Enzyme ◽  
High Level

Abstract. Faulina SA, Irfani M, Falah S, Hidayat A, Iswanto AH. 2020. Short Communication: The higher laccase enzyme producer, Cerrena sp. BMd. TA.1, isolated from Gunung Rinjani National Park, West Nusa Tenggara, Indonesia. Biodiversitas 21: 3837-3842. Lies in the Wallace line, Gunung Rinjani National Park (GRNP) offers unique biodiversity, fungi included. Fungal enzymes have been unceasingly searched and studied for various applications, particularly for biodegradation. Fungal laccase enzyme showed prospective environmental-friendly approach in treating industrial effluent, remazol brilliant blue R (RBBR) which is used as a synthetic dye. This study aimed to explore the laccase-producing fungi from the GNRP, as well as investigate their ability in decolorizing RBBR. The study discovered that the most prospective fungi isolate, molecularly identified as Cerrena sp. BMd.TA.1, produced a high level of laccase (> 2300 U mL-1) and manganese peroxidase (MnP, 300 U mL-1). In the application of this isolate, the laccase showed as predominant enzyme in RBBR decolorization process and the RBBR could be decolorized more than 80% at 24 h reaction. It suggested that Cerrena sp BMd.TA.1 isolate is highly potential as laccase enzyme producer and may be considered for further investigations in its applications for biodegradation, especially of dyes effluent.

scholarly journals Laccase Electrochemical Biosensor Based on Graphene-Gold/Chitosan Nanocomposite Film for Bisphenol A Detection

2020 ◽  
Vol 16 (5) ◽  
pp. 570-579
Author(s):  
Fuzi M. Fartas ◽  
Jaafar Abdullah ◽  
Nor A. Yusof ◽  
Yusran Sulaiman ◽  
Mohd I. Saiman ◽  
...  
Keyword(s):  
Bisphenol A ◽  
Electrochemical Biosensor ◽  
Limit Of Detection ◽  
Modified Electrodes ◽  
Electrochemical Performances ◽  
Carbon Electrode ◽  
Screen Printed Carbon Electrode ◽  
Laccase Enzyme ◽  
Bisphenol A Detection ◽  
Screen Printed

Background: Bisphenol A (BPA) is considered one of the most common chemicals that could cause environmental endocrine disrupting. Therefore, there is an increasing demand for simple, rapid and sensitive methods for BPA detection that result from BPA leaching into foods and beverages from storage containers. Herein, a simple laccase electrochemical biosensor was developed for the determination of BPA based on Screen-Printed Carbon Electrode (SPCE) modified graphenegold/ chitosan. The synergic effect of graphene-gold/chitosan nanocomposite as electrode modifier greatly facilitates electron-transfer processes between the electrolyte and laccase enzyme, thus leads to a remarkably improved sensitivity for bisphenol A detection. Methods: In this study, laccase enzyme is immobilized onto the Screen-Printed Carbon Electrode (SPCE) modified Graphene-Decorated Gold Nanoparticles (Gr-AuNPs) with Chitosan (Chit). The surface structure of nanocomposite was studied using different techniques including Field Emission Scanning Microscopy (FESEM), TRANSMISSION Electron Microscopy (TEM), Raman spectroscopy and Energy Dispersive X-ray (EDX). Meanwhile, the electrochemical performances of the modified electrodes were studied using Cyclic Voltammetry (CV) and Differential Pulse Voltammetry (DPV). Results: The developed laccase biosensor offered excellent analytical performance for the detection of BPA with a sensitivity of 0.271 μA/μM and Limit of Detection (LOD) of 0.023 μM, respectively. Moreover, the constructed biosensor showed good reproducibility, selectivity and stability towards BPA. The sensor has been used to detect BPA in a different type of commercial plastic products as a real sample and satisfactory result was obtained when compared with the HPLC method. Conclusion: The proposed electrochemical laccase biosensor exhibits good result which is considered as a promising candidate for a simple, rapid and sensitive method especially in the resource- limited condition.

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