Novel Inhibitory Function of the Lipase Propeptide and Three-Dimensional Structures of Its Complexes with the Enzyme.

Many proteins are synthesized as precursors, with propeptides playing a variety of roles such as assisting in folding or preventing them from being active within the cell. While the precise role of the propeptide in fungal lipases is not completely understood, it was previously reported that mutations in the propeptide region of the lipase have an influence on the activity of the mature enzyme, stressing the importance of the amino acid composition of this region. We here report two structures of this enzyme in complex with its propeptide, which suggests that the latter plays a role in the correct maturation of the enzyme.

Purification and characterization of a peroxidase isozyme from Indian turnip roots.

A peroxidase isozyme (TP I) from Indian turnip roots ( Brassica rapa ) was purified. TP I had a minimum molecular mass of 45 000 Da as determined from sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). A far-UV circular dichroism (CD) spectroscopy study of TP I revealed the presence of 44% alpha-helix, 16% beta-sheet, and 40% random structure.

Purification and properties of the alkaline lipase from Burkholderia cepacia A.T.C.C. 25609.

A Burkholderia cepacia (bacteria) strain, A.T.C.

A multipurpose immobilized biocatalyst with pectinase, xylanase and cellulase activities.

Background: The use of immobilized enzymes for catalyzing various biotransformations is now a widely used approach. In recent years, cross-linked enzyme aggregates (CLEAs) have emerged as a novel and versatile biocatalyst design. The present work deals with the preparation of a CLEA from a commercial preparation, Pectinex Ultra SP-L, which contains pectinase, xylanase and cellulase activities.

Treatment of phenolic wastewater by horseradish peroxidase immobilized by bioaffinity layering.

Horseradish peroxidase was immobilized by bioaffinity layering and used for the treatment of wastewater containing p-chlorophenol. For this purpose, lectin Concanavalin A was bound to Sephadex beads. The glycoenzyme peroxidase was layered upon this Con A layer.