Anthraquinone
(AQ) compounds have been used as photolabile protecting
groups (PPGs) to protect alcohols, ketones, and carboxylic acids.
However, because of the lack of direct spectroscopic information for
the transient species and intermediates related with the deprotection
reaction(s), the photorelease mechanism(s) of these systems are still
largely unknown. In this contribution, we detail a time-resolved spectroscopic
investigation using anthraquinone-protected galactose (1) and adenosine (2) to investigate the photodeprotection
reaction mechanism(s) of these kinds of AQ-PPGs. It was found that,
in THF-H2O solvents, the ketyl radical species generated
for 1 and 2 was found to be a reactive intermediate
that then formed a dihydroxyanthracene species. The photodeprotection
then occurred with the accompaniment of a decarboxylation process.
These results provide an improved understanding for how AQ-PPGs work
and will help assist in the design and applications of selected anthraquinone
derivatives as a PPG platform, especially in aqueous environments
more relevant for use in biological systems.
Pleurotus ostreatus is a species of white-rot fungi that effectively degrades lignin. In this study, we aimed to efficiently express the lac-2 gene of Pleurotus ostreatus in the Pichia pastoris X33 yeast strain. The enzymatic properties of recombinant yeast were determined, and its ability to degrade corn stover lignin was determined. The results showed the optimum pH values of recombinant laccase for 2,2'-Azinobis-3-ethylbenzothiazoline-6-sulfonic acid, 2,6-dimethoxyphenol, and 2-methoxyphenol were 3.0, 3.0, and 3.5, respectively. The optimum reaction temperature was 50 • C, and it had good thermal stability and acid and alkali resistance. The degradation rate of lignin in corn stover by recombinant laccase was 18.36%, and the native Pleurotus ostreatus degradation rate was 14.05%, the difference between them is significant (p < 0.05). This experiment lays a foundation for the study of the degradation mechanism of lignin by laccase.
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