The protein structure determines the sensitizing capacity of Brazil nut 2S albumin (Ber e1) in a rat food allergy model.

: It is not exactly known why certain food proteins are more likely to sensitize. One of the characteristics of most food allergens is that they are stable to the acidic and proteolytic conditions in the digestive tract. This property is thought to be a risk factor in allergic sensitization.

Older adults and patients in need of nutritional support: review of current treatment options and factors influencing nutritional intake.

Background & Aims: Many older adults and patients do not achieve sufficient nutritional intake to support their minimal needs and are at risk of, or are suffering from, (protein-energy) malnutrition. Better understanding of current treatment options and factors determining nutritional intake, may help design new strategies to solve this multifactorial problem.

Methods: Medline, Science Citation Index, ScienceDirect and Google databases (until December 2008) were searched with the keywords malnutrition, elderly, older adults, food intake, energy density, variety, taste, satiety, and appetite.

Dietary sphingolipids lower plasma cholesterol and triacylglycerol and prevent liver steatosis in APOE*3Leiden mice.

Background: The prevalence of dyslipidemia and obesity resulting from excess energy intake and physical inactivity is increasing. The liver plays a pivotal role in systemic lipid homeostasis. Effective, natural dietary interventions that lower plasma lipids and promote liver health are needed.

Reversible denaturation of Brazil nut 2S albumin (Ber e1) and implication of structural destabilization on digestion by pepsin.

The high resistance of Brazil nut 2S albumin, previously identified as an allergen, against proteolysis by pepsin was examined in this work. Although the denaturation temperature of this protein exceeds the 110 degrees C at neutral pH, at low pH a fully reversible thermal denaturation was observed at approximately 82 degrees C. The poor digestibility of the protein by pepsin illustrates the tight globular packing.

Transglutaminase-mediated modification of glutamine and lysine residues in native bovine beta-lactoglobulin.

Bovine beta-lactoglobulin (BLG) is a major component in whey and its physical properties are important for the texture of many dairy-based foods. Modification of proteins with transglutaminase from Streptoverticillium mobaraense (MTGase) can be used to alter their physical properties. MTGase-mediated modification of native BLG was until now, however, not effective.

Modification of glutamine and lysine residues in holo and apo alpha-lactalbumin with microbial transglutaminase.

The molecular structures determine the physical properties of milk proteins and are important for the texture of many dairy-based foods. Bovine alpha-lactalbumin (alpha-LA) is a globular 123 amino acid Ca(2+) binding milk protein. Modification with microbial Ca(2+) independent transglutaminase (MTGase) was used to modify lysines and glutamines in holo and apo alpha-LA.

Molecular cloning and characterization of the alkaline ceramidase from Pseudomonas aeruginosa PA01.

Ceramidase (CDase) hydrolyzes the amide bond in ceramides to yield free fatty acid and sphingosine. From a 3-L Pseudomonas aeruginosa PA01 culture, 70 microg of extracellular alkaline, Ca(2+)-dependent CDase, was purified to homogeneity, the N-terminal sequence was determined, and the CDase gene was cloned. The CDase gene encodes a 670 amino acid protein with a 26 amino acid signal peptide.

Synthesis of a novel fluorescent ceramide analogue and its use in the characterization of recombinant ceramidase from Pseudomonas aeruginosa PA01.

Ceramidase (CDase) hydrolyses the N-acyl linkage of the sphingolipid ceramide. We synthesized the non-fluorescent ceramide analogue (4E,2S,3R)-2-N-(10-pyrenedecanoyl)-1,3,17-trihydroxy-17-(3,5-dinitrobenzoyl)-4-heptadecene (10) that becomes fluorescent upon hydrolysis of its N-acyl bond. This novel substrate was used to study several kinetic aspects of the recombinant CDase from the pathogenic bacterium Pseudomonas aeruginosa PA01.