|Yi Yang, Jinshui Yang, Baozhen Li, Entao Wang, Hongli Yuan. An esterase from Penicillium decumbens P6 involved in lignite depolymerization. Fuel. DOI: org/10.1016/j.fuel|
An esterase from Penicillium decumbens P6 involved in lignite depolymerization
Yi Yang, Jinshui Yang, Baozhen Li, Entao Wang, Hongli Yuan
In this study, lignite was degraded using a puriﬁed esterase from Penicillium decumbens P6 for the ﬁrst time. The esterase was puriﬁed using ammonium sulfate precipitation, anion exchange and gel ﬁltration chromatography. The recovery and puriﬁcation yield of the enzyme were 15% and 83 folds, respectively. The molecular weight of the puriﬁed enzyme was about 45kDa. Both crude and puriﬁed esterases were studied for lignite depolymerization. The tendency of depolymerization by crude enzyme was consistent with the enzyme secreted in the medium. Along with the increased puriﬁed esterase concentration from 8 to 50mg/ml, A450 value increased from 0.38to 2.08. Thecontribution ofesterase to the depolymerization was about 40%in thecrude supernatant. Compared with aHA (crude lignite humic acid), bHA (esterase degraded lignite humic acid) has a lower percentage of aromatic carbon and ester groups, but a higher percentage of aliphatic carbon. bHA can promote the growth of asparagus lettuce. The results demonstrated that lignite was depolymerized by the puriﬁed esterase and evidenced the potential of esterase application in conversion of lignite into compounds with high bioactivities.