Bioprocessing of laccase produced by submerged culture of Ganoderma sp. WR-1

Optimization of the production, purification and characterization of a laccase from the native fungus Xylaria sp.

“…The stability of the enzyme was higher towards pH values close to neutral and even slightly alkaline (6-9) (Fig.3a), which is also consistent with that observed for many laccases, with greater stability at pH values slightly above the laccase pI (Rajeeva and Lele, 2010). For example, Liers et al (2007) studied X. polymorpha and observed higher stability at pH 7-10 and at an enzyme pI of 3.1.…”

Partitioning of cerrena unicolor laccase activity in an aqueous two-phase system

“…According to Kula et al (1982), about 60-80% of all expenses in biotechnological processes are spent on downstream processing. Various conventional methods, such as micro-and ultrafiltration (Bryjak and Rekuć, 2009), chromatography (Yang et al, 2013), or precipitation (Rajeeva and Lele, 2010), have been employed for downstream processing of laccases. Unfortunately, those methods are highly inefficient in terms of yields and energy consumption.…”

A Laccase with Antiproliferative and HIV-I Reverse Transcriptase Inhibitory Activities from the Mycorrhizal FungusAgaricus placomyces

“…It is widely distributed among plants, insects, bacteria, and especially fungi [ 3 ]. With a research history of more than a century, laccase has gained importance as a versatile industrial enzyme with a repertoire of applications in lignin degradation, environmental detoxification, and a variety of industries including paper, textile, bioremediation, biocatalysis, diagnostic, and food industries [ 4 , 5 ]. Studies on laccases have mainly focused on characterization in terms of molecular mass, protein sequence, pH and temperature optima, enzyme kinetics, substrate specificity, purification protocol, cloning, structure, applications, and chemical synthesis [ 1 , 3 , 6 – 8 ].…”