Expression and purification of dalcochinase, a beta-glucosidase from Dalbergia cochinchinensis Pierre, in yeast and bacterial hosts.

The coding sequence of the mature dalcochinase, a beta-glucosidase from Dalbergia cochinchinensis Pierre, was cloned and expressed in various systems. Expression in Escherichia coli resulted in an insoluble protein, which could be made soluble by co-expression with bacterial chaperonin GroESL. However, the enzyme had no activity.

The hydrophobic domain 26 of human tropoelastin is unstructured in solution.

Elastin is the protein responsible for the elastic properties of vertebrate tissue. Very little is currently known about the structure of elastin or of its soluble precursor tropoelastin. We have used high-resolution solution NMR methods to probe the conformational preferences of a conserved hydrophobic region in tropoelastin, domain 26 (D26).