An Easy Method for Screening and Detection of Laccase Activity

Dias, Albino A.; Matos, António J.S.; Fraga, Irene; Sampaio, Ana; Bezerra, Rui M. F.

doi:10.2174/1874070701711010089

Cited by 10 publications

(5 citation statements)

References 13 publications

(10 reference statements)

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…1995; Dias et al . 2017). The production of extracellular LiP was observed by zone clearance around fungal colonies growing on methylene blue indicator dye (0·25 g l −1 ) containing potato dextrose agar plate.…”

Section: Methodsmentioning

confidence: 99%

Elucidation of fungal dye‐decolourizing peroxidase (DyP) and ligninolytic enzyme activities in decolourization and mineralization of azo dyes

Rajhans

Sen²,

Barik

et al. 2020

J Appl Microbiol

View full text Add to dashboard Cite

Aim The aim of the study is to investigate the efficiency of Geotrichum candidum in the decolourization and mineralization of synthetic azo dyes. Methods and Results It includes screening of enzymes from G. candidum and its optimization, followed by decolourization and mineralization studies. Decolourization was observed to be maximum in methyl orange (94·6%) followed by Congo red (85%), trypan blue (70·4%) and Eriochrome Black T (55·6%) in 48 h, suggesting the plausible degradation of the azo dyes by G. candidum. The enzyme activity study showed that DyP‐type peroxidase has highest activity of 900 mU ml−1 compared to that of laccase (405 mU ml−1) and lignin peroxidase (LiP) (324 mU ml−1) at optimized pH (6) and temperature (35°C). Moreover, the rate of decolourization was found to be directly proportional to the production of laccase and LiP, unlike DyP‐type peroxidase. Furthermore, mineralization study demonstrated reduction in aromatic amines, showing 20% mineralization of methyl orange. Conclusion Geotrichum candidum with its enzyme system is able to efficiently decolourize and mineralize the experimental azo dyes. Significance and Impact of the Study The efficient decolourization and mineralization of azo dyes makes G. candidum a promising alternative in the treatment of textile effluent contaminated with azo dyes.

show abstract

Section: Methodsmentioning

confidence: 99%

Elucidation of fungal dye‐decolourizing peroxidase (DyP) and ligninolytic enzyme activities in decolourization and mineralization of azo dyes

Rajhans

Sen²,

Barik

et al. 2020

J Appl Microbiol

View full text Add to dashboard Cite

show abstract

“…Laccase (EC 1.10.3.2) là một polyphenol oxidase có chứa cofactor là ion đồng, có khả năng oxy hóa đa dạng các hợp chất chứa vòng thơm như phenol, polyamin, và các aryl diamin cũng như một số các ion vô cơ, đặc biệt là lignin [4,5]. Ưu điểm vượt trội của laccase là có tính oxi hóa mạnh, sử dụng oxi phân tử làm chất nhận điện tử, vì vậy enzyme này có rất nhiều ứng dụng rộng rãi trong công nghiệp, như xử lý nguồn nước thải ô nhiễm bằng cách loại _______ * Tác giả liên hệ.…”

Section: Mở đầU *unclassified

Cloning, Experession, and Characterization of a Laccase from the White Rot Fungi Pleurotus pulmonarius MPN18

Quynh¹,

Hoang²,

Lan³

et al. 2023

NST

View full text Add to dashboard Cite

Laccase (EC 1.10.3.2) is an enzyme belonging to the polyphenol oxidase groups, which plays an important role in the oxidation of a wide variety of aromatic substrates, such as lignin, phenol, polyamine, and aryl diamines, as well as a number of other phenolic compounds or inorganic ions in the presence of oxygen. Laccase is widely applied in many different fields, especially in the textile industry, dyeing, and environmental pollution treatment. In this study, we have successfully cloned and expressed cDNA coding for laccase from Pleurotus pulmonarius MPN18 (PpLac). cDNA corresponds to the gene laccase (size 1566 bp) was attached to pET 21a(+) vector and expressed in E. coli BL21, after that the enzyme was purified through HisTrapTM sp 5mL column. The purified PpLac had an activity of 899.8 U, a 74% yield with a purity of 15.2 -fold, and was tested by SDS-PAGE electrophoresis with a molecular weight of Mw = 55 kDa. Enzyme displayed optimal activity at 50 ºC and pH 4.0. Enzyme had optimal activity of 20-40 ºC after 120 min incubation and pH 4 after 6 h incubation. In future, the recombinant enzyme will be characterized for supplementation into enzyme cocktail in the treatment of lignocellulosic material.

show abstract

“…But it has no copper I binding domain [ 251 ] Dias and colleagues [ 252 ] have reported a new zymogram dried 2,2’-azino-bis(3-ethylbenzo- thiazoline-6-sulfonic acid) (ABTS)-impregnated discs assay for laccase activity detection, which is associated with easy assay and rapid screening. The laccase activity was determined at a wavelength of 420 nm by measuring the oxidation of ABTS in phosphate citrate buffer at a pH value of 4.0 [ 253 ]. The other guaiacol assay has been reported for laccase assay by Kalra et al [ 254 ] to measure the reddish-brown color development at 450 nm as a consequence of the oxidation of guaiacol by Lac.…”

Section: Lignocellulolytic Enzyme Production By Mushroom Using Agrmentioning

confidence: 99%

Cultivation of Mushrooms and Their Lignocellulolytic Enzyme Production Through the Utilization of Agro-Industrial Waste

et al. 2020

View full text Add to dashboard Cite

A large amount of agro-industrial waste is produced worldwide in various agricultural sectors and by different food industries. The disposal and burning of this waste have created major global environmental problems. Agro-industrial waste mainly consists of cellulose, hemicellulose and lignin, all of which are collectively defined as lignocellulosic materials. This waste can serve as a suitable substrate in the solid-state fermentation process involving mushrooms. Mushrooms degrade lignocellulosic substrates through lignocellulosic enzyme production and utilize the degraded products to produce their fruiting bodies. Therefore, mushroom cultivation can be considered a prominent biotechnological process for the reduction and valorization of agro-industrial waste. Such waste is generated as a result of the eco-friendly conversion of low-value by-products into new resources that can be used to produce value-added products. Here, we have produced a brief review of the current findings through an overview of recently published literature. This overview has focused on the use of agro-industrial waste as a growth substrate for mushroom cultivation and lignocellulolytic enzyme production.

show abstract

An Easy Method for Screening and Detection of Laccase Activity

Cited by 10 publications

References 13 publications

Elucidation of fungal dye‐decolourizing peroxidase (DyP) and ligninolytic enzyme activities in decolourization and mineralization of azo dyes

Elucidation of fungal dye‐decolourizing peroxidase (DyP) and ligninolytic enzyme activities in decolourization and mineralization of azo dyes

Cloning, Experession, and Characterization of a Laccase from the White Rot Fungi Pleurotus pulmonarius MPN18

Cultivation of Mushrooms and Their Lignocellulolytic Enzyme Production Through the Utilization of Agro-Industrial Waste

Contact Info

Product

Resources

About