Background & Aims: Pancreatic exocrine insufficiency (PEI) impairs fat absorption, but few data are available on protein absorption. We investigated this question in patients with chronic pancreatitis, both in the absence and presence of enzyme therapy, using a stable isotope sensitive method.
Methods: Eleven patients with sustained PEI and regular enzyme substitution were investigated at hospital, after a washout period without enzyme substitution, and later after reintroduction of substitution. The digestibility and postprandial metabolism of dietary protein were characterized after the ingestion of a semi-synthetic single meal containing 20 g (15)N-labeled casein.
Results: At baseline, 20 ± 8% of dietary nitrogen was transferred to the metabolic pools vs. 24.5 ± 7% under enzyme treatment (P = 0.04). After treatment, the transfer of dietary nitrogen tended to increase in plasma amino acids, and increased significantly in plasma proteins and the deamination pool. In contrast, the fecal excretion of dietary nitrogen did not demonstrate any treatment effect. In patients not receiving insulin for diabetes, the treatment stimulated insulin secretion.
Conclusions: Protein malabsorption was mostly undetectable using standard fecal tests. The study of the postprandial fate of dietary protein revealed a moderate increase of its transfer to metabolic pools after enzyme substitution.
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http://dx.doi.org/10.1016/j.clnu.2011.06.006 | DOI Listing |
Chembiochem
January 2025
Department of Chemical Engineering and Applied Chemistry, University of Toronto, 200 College Street, Toronto, Ontario, M5S 3E5, Canada.
This study describes an enzymatic pathway to produce high purity 4-O-methylglucaric acid from xylan, an underutilized fraction of lignocellulosic biomass. Beechwood xylan was enzymatically hydrolysed using a commercial xylanase and an α-glucuronidase from Amphibacillus xylanus to form 4-O-methylglucuronic acid, which was then purified by anion exchange chromatography and subsequently oxidized to 4-O-methylglucaric acid using a recombinantly produced uronic acid oxidase from Citrus sinensis. Enzymatic oxidation with uronic acid oxidase afforded 95 % yield in 72 hours which is considerably higher than yields previously achieved using a glucooligosaccharide oxidase from Sarocladium strictum.
View Article and Find Full Text PDFFuture Med Chem
January 2025
Chemistry Department, Faculty of Science, Arish University, Arish, Egypt.
Background: Using an analogue-based drug design approach, a number of novel 2-substituted-1,3-thiazolone derivatives (3-10) have been produced and given permission to proceed for their anti-inflammatory properties. In the present paper, the new thiazole derivatives were designed, synthesized, and tested for their alpha-glucosidase, alpha-amylase, and COX-inhibitory activities. Approving the anti-diabetic activity.
View Article and Find Full Text PDFBioorg Chem
January 2025
Chemistry Department, Faculty of Science, Arish University, Al-Arish 45511, Egypt.
The search for new anticancer compounds is a major focus for researchers in chemistry, biology, and medicine. Cancer affects people of all ages and regions, with rising incidence rates. It does not discriminate by age or gender, making it a significant threat to humanity.
View Article and Find Full Text PDFAnn Clin Microbiol Antimicrob
January 2025
Division of Infectious Diseases, Department of Internal Medicine, National Taiwan University Hospital, 7 Chung-Shan South Road, Taipei, 100, Taiwan.
Background: Nemonoxacin is a new quinolone with an antibacterial efficacy against methicillin-resistant Staphylococcus aureus (MRSA). Certain sequence types (STs) have been emerging in Taiwan, including fluoroquinolone-resistant ST8/USA300. It's an urgent need to determine nemonoxacin susceptibility against ST8/USA300 and other emerging lineages, if any.
View Article and Find Full Text PDFBiochimie
January 2025
Engelhardt Institute of Molecular Biology of the Russian Academy of Sciences, Vavilov street, 32, Moscow, 119991, Russia.
Pyridoxal 5'-phosphate (PLP)-dependent enzymes are involved in many cellular processes and possess unequalled catalytic versatility. Rational design through site-directed mutagenesis is a powerful strategy for creating tailor-made enzymes for a wide range of biocatalytic applications. PLP-dependent methionine γ-lyase (MGL), which degrades sulfur-containing amino acids, is an encouraging enzyme for many therapeutic purposes - from combating bacterial resistant strains and fungi to antitumor activity.
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