Jellynolide A, pokepola esters, and sponalisolides from the aquaculture sponge Spongia officinalis L.

Jellynolide A, an unreported bicyclic diterpenoid with an unprecedented penta-substituted carbon skeleton which implied an irregular biogenic pathway, together with four pairs of rare phosphate triesters, (±)-pokepola ester B-E, one undescribed related racemic furanoterpenoid, (±)-sponalisolide C, one undescribed furanoterpenoid, (-)-sponalisolide D, and two known (±)-sponalisolide B and dendrolasin carboxylic acid were isolated from the aquaculture Spongia officinalis L. Their structures were elucidated by comprehensive spectroscopic analysis, quantum chemical calculation of NMR parameters, and electronic circular dichroism (ECD). The plausible biosynthetic pathway of jellynolide A was proposed. (±)-Pokepola ester C exhibited significant inhibition against Wnt, HIF1 signaling pathways. (+)-Pokepola ester B and (-)-pokepola ester D showed moderate cytotoxicity activities.

Enhancement of catalytic activity and thermostability of a thermostable cellobiohydrolase from Chaetomium thermophilum by site-directed mutagenesis.

Enzymatic saccharification of lignocellulosic biomass is increasingly applied in agricultural and industrial applications. Nevertheless, low performance in the extreme environment severely prevents the utilization of commercial enzyme preparations. To obtain cellobiohydrolases with improved catalytic activity and thermostability, structure-based rational design was performed based on a thermostable cellobiohydrolase CtCel6 from Chaetomium thermophilum. In the present study, four conserved and noncatalytic residue substitutions were generated via site-directed mutagenesis. Mutations were heterologously expressed in yeast Pichia pastoris, purified, and ultimately assayed for enzymatic characteristics. The mutant Y119F increased the catalytic activity 1.82-, 1.65- and 1.43-fold against ß-d-glucan, phosphoric acid swollen cellulose (PASC) and carboxymethylcellulose sodium (CMC-Na), respectively. In addition, S131 W effectively enhanced the enzyme's heat resistance to elevated temperatures. The half-life (t1/2) of this mutant enzyme was increased 1.42- and 2.40-fold at 80 °C and 90 °C, respectively, compared to the wild-type. This study offers initial insight into the biological function of the conserved and noncatalytic residues of thermostable cellobiohydrolases and provides a valid approach to the improvement of enzyme redesign proposal.

Lasing and magnetic microbeads loaded with colloidal quantum dots and iron oxide nanocrystals.

This study investigates the feasibility of loading nanostructured lasing medium and magnetic nanocrystals in the same microbead for potential applications in bio- and chemical sensing. A sequential infiltration process is proposed and tested for the preparation of magnetic and lasing microbeads by incorporating, respectively, iron oxide nanocrystals in the inner cores and colloidal quantum dots (CQDs) in the periphery regions of mesoporous silica microbeads. The co-doped bead structure was confirmed by electron microscopy and energy dispersive spectroscopy. The lasing action of the CQD gain medium in the mesoporous beads was characterized with micro-photoluminescence, revealing sharp whispering gallery mode lasing signatures, whereas the distinguishing superparamagnetic property was measured from the co-doped microbeads with vibrating sample magnetometry.