Abstract
Laccases are an interesting group of multi copper enzymes, which have received much attention of researchers in the last decades due to their ability to oxidise both phenolic and nonphenolic lignin-related compounds as well as highly recalcitrant environmental pollutants. This makes these biocatalysts very useful for their application in several biotechnological processes, including the food industry. Thus, laccases hold great potential as food additives in food and beverage processing. Being energy-saving and biodegradable, laccase-based biocatalysts fit well with the development of highly efficient, sustainable, and eco-friendly industries.
Highlights
Laccases (p-diphenol:dioxygen oxidoreductases; EC 1.10.3.2) are abundant in white-rot fungi, which are the only organisms able to degrade the whole wood components [1]
Laccases are an interesting group of multi copper enzymes, which have received much attention of researchers in the last decades due to their ability to oxidise both phenolic and nonphenolic lignin-related compounds as well as highly recalcitrant environmental pollutants
Bitterness and other unpleasant tastes were removed by the laccase treatment, and the chocolate manufactured from the cacao mass tasted better than the control
Summary
Laccases (p-diphenol:dioxygen oxidoreductases; EC 1.10.3.2) are abundant in white-rot fungi, which are the only organisms able to degrade the whole wood components [1]. The substrates of interest cannot be oxidised directly by laccases, either because they are too large to penetrate into the enzyme active site or because they have a high redox potential. The role of laccases is to degrade lignin in order to gain access to the other carbohydrates in wood (cellulose and hemicellulose) Their low substrate specificity allows laccases to degrade compounds with a structure similar to lignin, such as polyaromatic hydrocarbons (PAHs), textile dyes, and other xenobiotic compounds [2]. Typical fungal laccases are extracellular proteins of approximately 60–70 kDa with acidic isoelectric point around pH 4.0 [5] They are generally glycosylated, with an extent of glycosylation ranging between 10 and 25% and only in a few cases higher than 30% [6, 7]. The utilisation of whole laccase-producing microorganisms is not considered in the present paper
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