Highlights d Budding yeast G2-cyclin Clb3 uses a PxxPxF motif for specific substrate targeting d PxxPxF promotes Ypr174c phosphorylation to recruit Polo kinase Cdc5 to centrosomes d Hydrophobic patch of cyclins can bind both exclusive and universal docking motifs d Elements around the docking motifs tune their specificity for yeast and human CDKs

Lignin is an abundant and renewable source capable of replacing different raw materials in the chemical industry. It can be obtained from lignocellulosic biomass (LCB) via different pretreatment methods. In the present study, hydrolysis lignin (HL) from the SunburstTM pretreatment technology was utilized to investigate its enzymatic conversion. At first, soluble HL fractions were obtained via alkali solubilization followed by acid precipitation, referred to as acid precipitated lignin (APL). Furthermore, the APL was tested with three different bacterial laccases to identify the optimal conditions for its conversion into small molecular weight fractions. Among the tested laccases, Streptomyces coelicolor A3(2) (ScLac) displayed the highest rate of APL conversion with a high lignin dosage and under extremely alkaline conditions, i.e., 50 g/L in 0.25 M NaOH solution, resulting in higher molecular weight fractions. The increase in the molecular weight and quantitative linkages before and after the enzymatic oxidation of the APL were characterized by size exclusion chromatography (SEC), Fourier-transform infrared spectroscopy (FT-IR), and two-dimensional heteronuclear single quantum correlation nuclear magnetic resonance (2D HSQC NMR) methods.

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