secale strictum/carbohydrate

To assess the effects of content and structure of dietary fiber (DF) on the carbohydrate digestibility and physicochemical properties of ileal digesta, five bread diets were studied in an experiment with ileum-cannulated pigs in a crossover design. The diets consisted of two experimental breads

Different extraction, purification and digestion methods were used to investigate the molecular properties of carbohydrates in arabinoxylan and β-glucan concentrates, dietary fiber (DF) rich breads and ileum content of bread fed pigs. The breads studied were: a low DF wheat bread (WF), whole meal

Eleven adults of both sexes ate a low-carbohydrate diet consisting mainly of meat, fish, and eggs for two days. After a low-carbohydrate breakfast on the third day, they operated a Stressalyzer to test their basic perceptual motor skill. Each subject drank 1.5 oz. rye whiskey at hourly intervals

Four experiments were conducted with laying hens and one with broiler chicks to investigate the effect of carbohydrate source on fat accumulation in the liver. When corn and wheat in various proportions were fed to laying hens, the percent fat and total fat per liver increased as the proportion of

BACKGROUND Diets rich in whole-grain cereals and foods with a low glycemic index may protect against type 2 diabetes, but the underlying molecular mechanisms are unknown. OBJECTIVE The main objective was to test whether 2 different carbohydrate modifications--a rye-pasta diet characterized by a low

Energy balances of cocks and chickens were measured using the nitrogen-carbon-balance method. In Experiment 1 twelve adult White Leghorn cocks were fed alternately on a basal ration or on a supplemental ration composed of 75% basal diet and 25% carbohydrate source as a supplement. In Experiment 2

OBJECTIVE Whole-grain cereals and diets with a low glycemic index may protect against the development of type 2 diabetes and heart disease, but the mechanisms are poorly understood. We studied the effect of carbohydrate modification on serum metabolic profiles, including lipids and branched chain

Carbohydrates have long been recognized as an important aspect of freezing tolerance in plants but the association between these two factors is often ambiguous. To help clarify the relationship, the allocation of carbohydrates between specific tissues within the over wintering organ (crown) of

Grass and mite allergens are of the main causes of allergy and asthma. A carbohydrate-binding module (CBM) represents a common motif to groups I (β-expansin) and II/III (expansin-like) grass allergens and is suggested to mediate allergen-IgE binding. House dust mite group II allergen (Der p 2 and

(1) Cellulases and xylanases display a modular architecture that comprises a catalytic module linked to one or more non-catalytic carbohydrate-binding modules (CBMs). On the basis of primary structure similarity, CBMs have been classified into more than 30 different families. These non-catalytic

Six pigs of initial weight 40 +/- 1.7 kg with a T-piece cannula fitted at the terminal ileum were given diets composed of 96.3% of rye, barley or triticum grains ground to pass the 2.6 mm mesh, 3.3% mineral and vitamin mixture and 0.4% Cr2O3. Each diet was given to all pigs in a Latin square design,

The carbohydrate component of Glycoprotein 2 (12% carbohydrate) from rye-grass (Lolium perenne) pollen has saccharide sequences that contribute to its antigenicity. Radioimmunoassay inhibition tests show that the antiserum to this glycoprotein cross-reacts with a number of other plant glycoproteins.

The gene encoding the family 6 carbohydrate-binding module (CtCBM6A) from Clostridium thermocellum, cloned in pET-21a(+) expression vector, was overexpressed using Escherichia coli BL-21(DE3) cells and purified by immobilized metal-ion affinity chromatography. SDS-PAGE analysis of the recombinant

CtCBM6 of glucuronoxylan-xylanohydrolase (CtXynGH30) from Clostridium thermocellum was cloned, expressed and purified as a soluble ~14 kDa protein. Quantitative binding analysis with soluble polysaccharides by affinity electrophoresis and ITC revealed that CtCBM6 displays similar affinity towards

Ruminiclostridium josui Fae1A is a modular enzyme consisting of an N-terminal signal peptide, family-1 carbohydrate esterase module (CE1), family-6 carbohydrate-binding module (CBM6), and dockerin module in that order. Recombinant CE1 and CBM6 polypeptides were collectively and separately produced