Effective melanin degradation by a synergistic laccase-peroxidase enzyme complex for skin whitening and other practical applications

Shin, Seung-Soo; Hyeon, Jeong Eun; Joo, Young-Chul; Jeong, Da Woon; You, Sung Hyun; Han, Sung Ok

doi:10.1016/j.ijbiomac.2019.02.027

Cited by 39 publications

(25 citation statements)

References 27 publications

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“…Laccase (benzenediol: oxygen oxidoreductase, EC 1.10.3.2), belonging to a group of enzymes called multicopper blue oxidasehas been noted to exhibit a wide substrate specificity [1]. It has been applied in various sectors, such as biomedical [2], dye degradation [3], paper industries for delignification [4][5], bioremediation [6], in biosensors [7], as melanin degraders in the cosmetic industry [8], as an enzymatic biofuel [9] and used in juice clarification [10]. Furthermore, laccase is a key biological mediator and the best alternative for chemical mediators; thus, it is regarded as a green enzyme in dye degradation, which is a new era for dye degradation [11].…”

Section: Introductionmentioning

confidence: 99%

Tree bark scrape fungus: A potential source of laccase for application in bioremediation of non-textile dyes

Sayyed

Bhamare²,

Sapna

et al. 2020

PLoS ONE

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Although laccase has been recognized as a wonder molecule and green enzyme, the use of low yielding fungal strains, poor production, purification, and low enzyme kinetics have hampered its large-scale application. Thus,this study aims to select high yielding fungal strains and optimize the production, purification, and kinetics of laccase of Aspergillus sp. HB_RZ4. The results obtained indicated that Aspergillus sp. HB_RZ4 produced a significantly large amount of laccase under meso-acidophilic shaking conditions in a medium containing glucose and yeast extract. A 25 μM CuSO 4 was observed to enhance the enzyme yield. The enzyme was best purified on a Sephadex G-100 column. The purified enzyme resembled laccase of A. flavus. The kinetics of the purified enzyme revealed high substrate specificity and good velocity of reaction,using ABTS as a substrate. The enzyme was observed to be stable over various pH values and temperatures. The peptide structure of the purified enzyme was found to resemble laccase of A. kawachii IFO 4308. The fungus was observed to decolorize various dyes independent of the requirement of a laccase mediator system. Aspergillus sp. HB_RZ4 was observed to be a potent natural producer of laccase, and it decolorized the dyes even in the absence of a laccase mediator system. Thus, it can be used for bioremediation of effluent that contains non-textile dyes.

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Section: Introductionmentioning

confidence: 99%

Tree bark scrape fungus: A potential source of laccase for application in bioremediation of non-textile dyes

Sayyed

Bhamare²,

Sapna

et al. 2020

PLoS ONE

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“…Compared with pure laccase, the number of melanin particles increased the specific binding of melanin by 64%, and the degradation efficiency is 6.4 times higher than that of the former. As a new generation of whitening additives, it has a great industrial application potential [39]. The research on the DyP biosensor, such as hydrogen peroxide biosensor, DyP has a unique advantage.…”

Section: Other Potential Applicationsmentioning

confidence: 99%

Dye Decoloring Peroxidase Structure, Catalytic Properties and Applications: Current Advancement and Futurity

Xu¹,

Sun²,

Qaria³

et al. 2021

Catalysts

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Dye decoloring peroxidases (DyPs) were named after their high efficiency to decolorize and degrade a wide range of dyes. DyPs are a type of heme peroxidase and are quite different from known heme peroxidases in terms of amino acid sequences, protein structure, catalytic residues, and physical and chemical properties. DyPs oxidize polycyclic dyes and phenolic compounds. Thus they find high application potentials in dealing with environmental problems. The structure and catalytic characteristics of DyPs of different families from the amino acid sequence, protein structure, and enzymatic properties, and analyzes the high-efficiency degradation ability of some DyPs in dye and lignin degradation, which vary greatly among DyPs classes. In addition, application prospects of DyPs in biomedicine and other fields are also discussed briefly. At the same time, the research strategy based on genetic engineering and synthetic biology in improving the stability and catalytic activity of DyPs are summarized along with the important industrial applications of DyPs and associated challenges. Moreover, according to the current research findings, bringing DyPs to the industrial level may require improving the catalytic efficiency of DyP, increasing production, and enhancing alkali resistance and toxicity.

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“…Applications of alkaline laccases for this purpose have been reported [63,106]. The ability of laccase to degrade melanin has also been proposed for skin-whitening applications [107].…”

Section: Pharma/cosmetics/agrochemicalsmentioning

confidence: 99%

Applications of Microbial Laccases: Patent Review of the Past Decade (2009–2019)

et al. 2019

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There is a high number of well characterized, commercially available laccases with different redox potentials and low substrate specificity, which in turn makes them attractive for a vast array of biotechnological applications. Laccases operate as batteries, storing electrons from individual substrate oxidation reactions to reduce molecular oxygen, releasing water as the only by-product. Due to society’s increasing environmental awareness and the global intensification of bio-based economies, the biotechnological industry is also expanding. Enzymes such as laccases are seen as a better alternative for use in the wood, paper, textile, and food industries, and they are being applied as biocatalysts, biosensors, and biofuel cells. Almost 140 years from the first description of laccase, industrial implementations of these enzymes still remain scarce in comparison to their potential, which is mostly due to high production costs and the limited control of the enzymatic reaction side product(s). This review summarizes the laccase applications in the last decade, focusing on the published patents during this period.

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Effective melanin degradation by a synergistic laccase-peroxidase enzyme complex for skin whitening and other practical applications

Cited by 39 publications

References 27 publications

Tree bark scrape fungus: A potential source of laccase for application in bioremediation of non-textile dyes

Tree bark scrape fungus: A potential source of laccase for application in bioremediation of non-textile dyes

Dye Decoloring Peroxidase Structure, Catalytic Properties and Applications: Current Advancement and Futurity

Applications of Microbial Laccases: Patent Review of the Past Decade (2009–2019)

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