Phenolic colorants obtained by enzymatic synthesis using a fungal laccase in a hydro-organic biphasic system

Mustafa, Rana; Muniglia, Lionel; Rovel, B.; Girardin, Michel

doi:10.1016/j.foodres.2005.02.019

Cited by 76 publications

(52 citation statements)

References 17 publications

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“…Previously, we investigated ferulic acid oxidation by Myceliophthora thermophila laccase to synthesize 'nature identical' stable pigments that could be used in cosmetics and foods [10]. In aqueous medium, the rate of ferulic acid conversion (0-60min) decreased from 5-0.5mm with negligible yield of yellow colour products, due to the higher activity of both enzyme and semi-quinones radical [10].…”

Section: /5mentioning

confidence: 99%

“…In aqueous medium, the rate of ferulic acid conversion (0-60min) decreased from 5-0.5mm with negligible yield of yellow colour products, due to the higher activity of both enzyme and semi-quinones radical [10]. Recently, a purified Myceliophthora thermophila laccase was used as a biocatalyst to enzymatic ally oxidize ferulic acid in aqueous medium using an eco-friendly procedure to synthesize new active molecules [17].…”

Section: /5mentioning

confidence: 99%

“…Considerable attention has been devoted to laccases as potential industrial enzymes in various applications, such as pulp delignification, wood fiber modification, dye or stain bleaching, chemical or medicinal synthesis, and contaminated water or soil remediation [5][6][7][8]. Furthermore, laccases can also be used in the food industry such as beverage (wine, fruit juice and beer) processing, sugar beet pectin gelatin, baking, food antioxidant and colorants synthesis [9,10].…”

Section: Introductionmentioning

confidence: 99%

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A Comparison of Spectrophotometric and Oxidoreduction Potential Method for Laccase Activity Measurement

Mustafa¹

2017

RMES

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Polyphenol oxidases (PPOs) oxidize phenolic compounds forming quinones, which undergo non-enzymatic reactions resulting in colored compounds. We studied ferulic acid and catechol oxidation by Myceliophthora thermophila laccases using oxidoreduction potential (ORP or Eh) as a novel method to determine PPO activity compared to the traditional spectrophotometric method. Eh varied time-dependently on ferulic acid and catechol concentrations. Eh increased to a maximum value (Eh max ), then decreased irreversibly proportional with substrate concentration. The ΔEh curves of ferulic acid and catechol oxidation at different concentrations by laccase exhibited two steps substrate oxidation: enzymatic and non-enzymatic; linear segments with increasing and decreasing slopes (rate of ΔEh change). The K m values determined spectrophotometrically and ORP were 0.55, 0.75 and 0.39, 0.32mM for catechol and ferulic acid, respectively. The kinetic parameters (K m , V max ) of enzymatic reaction were not significantly different between the spectrophotometry and ORP methods. The ORP method is simple, low-cost and fast enabling the differentiation between the enzymatic and nonenzymatic phenol oxidation reactions.

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Section: /5mentioning

confidence: 99%

Section: /5mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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A Comparison of Spectrophotometric and Oxidoreduction Potential Method for Laccase Activity Measurement

Mustafa¹

2017

RMES

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“…The synthesis of new colorants by laccase are currently developed from phenolic and polyphenolic compounds [19].…”

Section: Applications Of Laccase In the Textile Industrymentioning

confidence: 99%

Biotechnological applications of laccases in the textile industry

Mojsov

2014

Savr tehnol

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Owing to the specific nature, enzymes have become an important class of biochemicals in textile processing. The use of enzymes in the textile processing is rapidly gaining globally recognition because of their non-toxic and eco-friendly characteristics to reduce pollution in the textile production. The search for efficient technologies has increased the interest in the use of enzymes to substitute conventional chemical textile processes by environment-friendly and economically attractive bioprocesses. Furthermore, the use of enzymes results in reduced process times, energy and water savings, the improved product quality and the potential process integration. Among the different existing oxidant enzymes, laccases have been the subject of the intensive research in the last decades. Laccases are Oxidoreductase class of enzymes (benzenediol: EC 1.10.3.2). Laccases are generally active at pH 3-5 and in the optimal temperature range of 30-50 ºC. They oxidize by using molecular oxygen as an electron acceptor from the substrate. Laccases are used to bleach textiles, can be used for textile dyeing/finishing, and many other industrial, environmental uses. This review mainly focuses on the use of laccases as an alternate technology to the conventional methods.

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“…Potencijalna polja primjene su sinteza prirodnih proizvoda kao što su pigmenti i antioksidansi preko dimerizacije fenolnih i nefenolnih kiselina (Mustafa et al, 2005). Trenutno su lakaze iz gljiva jedine koje se koriste u industrijskim procesima (Xu et al, 2007).…”

Section: Slika 4 Katalitiĉki Ciklus Lakaze Modifikovano Iz Solomon unclassified

Removal of phenols and dyes from wastewater using native and recombinant oxidative enzymes

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Phenolic colorants obtained by enzymatic synthesis using a fungal laccase in a hydro-organic biphasic system

Cited by 76 publications

References 17 publications

A Comparison of Spectrophotometric and Oxidoreduction Potential Method for Laccase Activity Measurement

A Comparison of Spectrophotometric and Oxidoreduction Potential Method for Laccase Activity Measurement

Biotechnological applications of laccases in the textile industry

Removal of phenols and dyes from wastewater using native and recombinant oxidative enzymes

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