Combining solid dispersion-based spray drying with cyclodextrin to improve the functionality and mitigate the beany odor of pea protein isolate.

The beany flavor of pea protein limits its application in the food industry. This study aimed at addressing this problem by combining the advantages of solid-based spray drying technique and the ability of cyclodextrins (CD) to entrap volatiles. Pea protein isolates (PPI) was extracted by alkaline extraction-isoelectric precipitation, followed by co-spray drying with CD.

Medical nutrition: a comprehensive, school-wide curriculum review.

Background: A school-wide nutrition program was established in 1982 and a required medical nutrition course (MNC) was established in 1985 at the University of Nevada School of Medicine. Emphasis was placed on developing an integrated curriculum and on using innovative methods to incorporate nutrition into the existing curriculum.

Objective: The objective of this review was to establish a baseline and make positive curricular changes to comply with the recommendations of the Liaison Committee on Medical Education for accreditation.

Inactivation of GDP-mannose dehydrogenase from Pseudomonas aeruginosa by penicillic acid identifies a critical active site loop.

The pathogenic bacterium Pseudomonas aeruginosa synthesizes alginate as one of a group of virulence factors that are produced during infections. The enzyme GDP-mannose dehydrogenase catalyzes the committed step in alginate biosynthesis. We show here that penicillic acid is an irreversible inactivator of GDP-mannose dehydrogenase.

Disentangling the web of allosteric communication in a homotetramer: heterotropic inhibition of phosphofructokinase from Bacillus stearothermophilus.

A strategy for isolating each of the four potentially unique heterotropic pairwise allosteric interactions that exist in the homotetramer phosphofructokinase from Bacillus stearothermophilus is described. The strategy involves the construction of hybrid tetramers containing one wild-type subunit and three mutant subunits that have been modified to block binding of both the substrate, fructose 6-phosphate (Fru-6-P), and the allosteric inhibitor, phospho(enol)pyruvate (PEP). Each type of binding site occurs at a subunit interface, and mutations on either side of the interface have been identified that will greatly diminish binding at the respective site.