laccase

Laccase activity was not detected at any stage of development.

Laccase activity reached a maximum in cultures after 120 h.

Laccase is also responsible for wine developing an unacceptable flavour.

Also the use of enzymes such as the enzyme laccase is under investigation.

The dough became softer and this is related to laccase mediation.

Inactivation of laccase should be optimal with low temperature heat treatment.

Removal of type 1 copper causes a decrease in laccase activity.

If your juice turns brown, even with good free SO2 levels, then suspect laccase.

Under stressed conditions, temperature and medium, laccase secretion was increased.

C. unicolor has been identified as a source of the enzyme laccase.

In addition, two to three laccase isoforms were detected.

The optimized substrate formulation for laccase production was then calculated.

C. cinerea produces a variety of the same laccase, known as isoenzymes.

Laccase treated dough had low stability over prolonged storage.

P. conchatus, however, contains a white laccase that lacks the typical blue copper color.

This fungi is studied in the production of laccase for use in biotechnology.

A laccase gene cglcc1 from this fungus has been cloned and sequenced.

Laccase levels are shown in activity units.

Laccase can be eliminated by sorting the grapes.

Laccase is able to catalyze ring cleavage of aromatic compounds.

Laccase can be added to the wort or at the end of the process to remove the polyphenols that may still remain in beer.

Laccase can also remove excess oxygen in beer and increase the storage life of beer.

Laccase activity was detected only in conidiating cultures.

Laccase is very slowly degraded in wine.

Laccase has been proposed to delay the oxidation of polyphenols and stabilize the juice.