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At least 19 recordsLinked to original sources

PubMed2004

The effect of fat type, carbohydrase, and lipase addition on growth performance and nutrient utilization of young broilers fed wheat-based diets.

A 2 x 2 x 2 factorial experiment was conducted to evaluate the effects of fat type (beef tallow [50 g/kg diet] or canola oil [50 g/kg of diet]), carbohydrase addition (none or carbohydrases [0.4 g/kg diet]), and lipase addition (none or lipase [0.2 g/kg of diet]) on growth performance and nutrient utilization of male broilers fed a wheat-based diet from 5 to 18 d. The carbohydrase supplement contained xylanase, glucanase, cellulase, and other enzyme activities. The experimental diets were formulated to be suboptimal in major nutrients and each was fed in a mash form to 10 replicate pens of 5 broilers per pen. Body weight gain was not affected by fat type but a poorer feed/gain ratio (P < 0.001) was noted for tallow-containing diets. Regardless of fat type, carbohydrase enzyme supplementation improved (P < 0.001) BW gain and feed/gain ratio. There was no effect of lipase addition on chicken performance and nutrient utilization. When compared with canola oil, tallow-containing diets had a lower (P < 0.001) apparent fat digestibility and consequently a lower dietary AMEn content. Carbohydrase enzyme addition improved (P < 0.001) fat, starch, nitrogen, and nonstarch polysaccharide (NSP) digestibilities in the small intestine, improved AMEn, and reduced (P < 0.001) jejunal digesta viscosity in both fat types. Carbohydrase supplementation increased water-soluble (P < 0.001) and decreased water-insoluble (P < 0.001) NSP concentrations in the small intestine. The interaction between fat type and carbohydrase addition was only significant for fat digestibilities, with greater improvements seen for diets containing tallow. Significant interactions between carbohydrase addition and intestinal segment were noted for fat, starch, nitrogen, and NSP digestibilities, with the enzyme effects being greater in the jejunum than the ileum. It is evident from the present study that an appropriate carbohydrase preparation could eliminate the negative effects of soluble NSP on animal fat utilization in a wheat-based broiler diet.

Animal Nutritional Physiological Phenomena↗

PubMed1983

Effect of concentrate feeding on the bovine intestinal and pancreatic carbohydrases. Evidence of induced increase in their activities.

1. The effects of concentrate feeding on the levels and pattern of distribution of carbohydrases in bovine intestine and pancreas were investigated. 2. No remarkable difference was noticed in the pattern of distribution of the carbohydrases along the bovine intestine, which was mostly confined to the proximal part of the small intestine. 3. The concentrate feeding, however, highly affected the levels of carbohydrases in the mucosa, luminal contents and the pancreas. Their levels slightly decreased in the mucosal tissue and significantly increased in the luminal contents. In the pancreas, the level of amylase decreased and that of disaccharidases increased. 4. Based on the presence of higher levels of activities of carbohydrases in the luminal contents, supported by the concentrate-induced increase in their levels, it is argued that the site of carbohydrate digestion, including disaccharides, in the small intestine, is the luminal contents.

Animals↗

PubMed1975

Carbohydrase activity in the digestive system of some teleost fishes.

The activity of carbohydrases in Puntius sophore (Ham.), Channa gachua (Ham.) and Cirrhinus mrigala (Ham.) has been studied. The carbohydrases have been found in the stomach, intestinal bulb, intestine, pyloric caeca and the hepato-pancreas. The hepatopancreas is the main site of production of these enzymes and it is in this organ and the intestine that their activity is highest. Their pH optimum lies between 5.4 and 6.4. The enzyme equipment in the teleost is adapted to their respective food and feeding habits both qualitatively and quantitatively. In Puntius (omnivorous) and Cirrhinus (herbivorous) all three carbohydrases, namely amylase (EC 3.2.1.1.), sucrase (EC 3.2.1.26.) and raffinase, while in Channa (carnivorous) only amylase and sucrase have been found to be active. In Cirrhinus mrigala, which is predominantly a herbivorous species, the concentration of carbohydrases is higher than those in the other two fishes.

Animals↗

PubMed2000

A universal assay for screening expression libraries for carbohydrases.

Although many assays are available for the screening of expression libraries for carbohydrases, some enzymes cannot be detected because their substrates are incompatible with the existing assays. One thing that all carbohydrases have in common is that they increase the number of reducing ends when degrading their substrates. In this paper we explore the possibility of detecting this increase with the highly sensitive bicinchoninic acid (BCA) reducing value assay. This assay can be used for the detection of all carbohydrases degrading any polysaccharide; enzymes with either an exo- or an endo-type of mechanism can be detected at the same time. A cDNA library of Aspergillus tubigensis expressed in Kluyveromyces lactis clones, was screened with this assay for the presence of xylogalacturonan degrading enzyme(s). High background absorbances caused by culture medium, by proteins produced by the clones and by substrate could be dealt with by using the precautions described in this note. Three xylogalacturonase producing clones were found using this procedure.

Journal Article↗

PubMed2005

Degradation of cell wall polysaccharides by combinations of carbohydrase enzymes and their effect on nutrient utilization and broiler chicken performance.

In vitro incubation studies were carried out to determine if various carbohydrase preparations contained appropriate activities to target nonstarch polysaccharides (NSP) of wheat, soybean meal (SBM), canola meal, and peas. Triplicate samples (0.1 g) were incubated with a number of carbohydrase preparations (i.e., cellulase, pectinase, xylanase, glucanase, galactanase, and mannanase) or their combinations at 45 degrees C and pH 5.2. A more pronounced degradation of NSP was achieved when the enzyme preparations were used in concert. When compared with the control (nonenzyme treatment), the highest degree of NSP degradation reached was 37% for wheat, and 36, 26, and 28% for canola meal, SBM, and peas, respectively. Four enzyme combinations were studied further in a 2-wk (5 to 18 d of age) growth performance and nutrient digestibility trial with broiler chickens. All enzyme combinations were effective in improving (P < 0.05) weight gain, feed-to-gain ratio, AMEn, apparent ileal digestibilities of starch and protein, and apparent total tract digestibility of NSP in birds fed a wheat, wheat screening, SBM, canola meal, and peas-based diet. The most complex enzyme combination was found to be superior (P < 0.05) to others in improving ileal protein digestibility and feed-to-gain ratio. The effectiveness of this combination in elimination of the nutrient-encapsulating effect of cell walls was further evaluated in a balance study with adult roosters fed a conventionally ground full-fat canola seed. Enzyme addition increased (P < 0.05) NSP digestibility from 11.1 to 30.1%, which, in turn, resulted in a marked increase (P < 0.05) in TMEn value (4.176 vs 4.744 Mcal/kg) of the seed. It is evident from the present studies that the addition of an appropriate combination of carbohydrase enzymes to target cell wall polysaccharide structures could further improve enzyme efficacy in practical wheat, SBM, canola meal, and peas-based broiler diets.

Animal Nutritional Physiological Phenomena↗

PubMed1974

Effect of Glucose and Adenosine Phosphates on Production of Extracellular Carbohydrases of Alternaria solani.

Production of carbohydrases by Alternaria solani is inhibited by glucose under low growth conditions. In an enriched medium, glucose has little effect on the production of polygalacturonase and cellulase while it still suppresses production of beta-glucosidase. Low levels of all three enzymes were produced in the absence of their respective substrates. Such regulation has been found with many organisms. However, far greater production of these carbohydrases occurred with additions of adenosine phosphates to the growth media. Highest stimulation of enzyme production was by adenosine 5'-phosphate. Adenosine 5'-triphosphate and cyclic 3', 5'-adenosine monophosphate gave lesser amounts. Starvation appears to induce production of extracellular carbohydrases and adenosine 5'-phosphate may have a role in the starvation process.

Journal Article↗

PubMed1983

Dietary-induced rapid decrease of microvillar carbohydrase activity in rat jejunoileum.

Activities of several carbohydrases and peptidases were determined in proximal, middle, and distal thirds of the jejunoileum of female 16-wk-old rats that were fed a high-starch (70 cal%), low-fat (7 cal%) diet for 2 wk and also in rats that (after this introductory period) were fed an isocaloric low-starch (5 cal%), high-fat (73 cal%) diet for 1, 2, and 3 days. The body weight changes, food intake, amount of protein per intestinal segment, and rate of enterocyte migration were practically the same in all groups during these experimental periods. The decreased intake of starch was followed by a rapid decrease (40-80%) of carbohydrases (lactase, sucrase, maltase, and glucoamylase) within the first 24 h in total intestinal homogenates--and as studied in cryostat serial sections--in all regions of the jejunal villus-crypt columns, and mainly in proximal and middle segments. In contrast, the activities of leucylnaphthylamidase and L-phenylalanylglycine hydrolase exhibited little change except for a slight temporary decrease of activity on the 1st day in the proximal segment only (25-30%). Thus these data show that a decrease of starch content in an isocaloric diet evokes a rapid decrease in the activity of microvillar carbohydrases and that activity of these enzymes both in mature and immature enterocytes is capable of reacting to a change (decrease) of dietary carbohydrate content.

Animals↗

PubMed1990

Inhibitory effect of validamine, valienamine and valiolamine on activities of carbohydrases in rat small intestinal brush border membranes.

Three pseudo-aminosugars, validamine, valienamine and valiolamine, produced by Streptomyces hygroscopicus subsp. limoneus showed potent inhibitory action on rat small intestinal carbohydrase activities such as sucrase, maltase, glucoamylase, isomaltase and trehalase activities, but negligible action on lactase activity and pancreatic alpha-amylase activity. Where inhibition was seen, kinetic analysis showed fully competitive inhibition of the carbohydrase activities by all three inhibitors. Valiolamine has more potent carbohydrase inhibitory activity than validamine or valienamine, and the apparent Ki values of valiolamine for sucrase, maltase, glucoamylase, isomaltase and trehalase activities were 3.2 x 10(-7), 2.9 x 10(-6), 1.2 x 10(-6), 9.1 x 10(-7) and 4.9 x 10(-5) M, respectively, which are 10(-5) to 10(-3) times smaller than the apparent Km values.

Animals↗

PubMed2003

Use of carbohydrases in corn-soybean meal-based nursery diets.

Three experiments were conducted to test the hypothesis that supplementing nursery pig diets with a mixture of carbohydrases (CS) will improve pig performance and nutrient digestibility. The CS used in these experiments contained 7 units/g of alpha-1,6-galactosidase, 22 units/g of beta-1,4-mannanase, beta-1,4 mannosidase, and trace amounts of other enzymes. In Exp. 1, 108 pigs weaned at d 21 of age were fed one of three diets containing 0 (control), 0.1, or 0.2% CS for 5 wk, based on a three-phase feeding program (1, 2, and 2 wk). Over the entire 35-d period, ADG was not affected (P > 0.05) by treatment, but supplementing 0.1% CS increased (P < 0.05) gain:feed by 9%. Experiment 2 used 10 gilts fitted with simple T-cannula in the terminal ileum at 3 wk of age. After cannulation, pigs were fed the same control Phase I and II diets, but the Phase III diet contained either 0 or 0.1% CS. Ileal samples were collected for the 3 d following the 5-d adjustment period during Phase III. Apparent ileal digestibility of GE, lysine, threonine, and tryptophan was greater (P < 0.05) in the CS diet. In Exp. 3, 90 pigs weaned at 21 d of age were fed the same control Phase I and II diets, but the Phase III diet contained either 0 or 0.1% CS. Phase III diets were fed for 3 wk. Average daily gain of the CS group was greater (P < 0.05) than the control group during wk 3. Gain:feed ratio was greater (P < 0.05) for the carbohydrase group during the entire Phase III period. Four pigs per treatment were killed at the end of Exp. 3 to measure villus height and to determine the concentration of raffinose and stachyose in different parts of the gastrointestinal tract. Average villus height was greater (P < 0.05) in pigs fed the CS diet. Carbohydrase supplementation decreased (P < 0.05) the concentration of stachyose in freeze-dried digesta from the proximal and distal small intestine. Raffinose concentration, on the other hand, was decreased (P < 0.05) by CS supplementation only in the distal small intestine. These lower concentrations suggest that CS improved the digestibility of carbohydrate in soybean meal. In conclusion, the addition of CS to Phase I and Phase II nursery diets containing low levels of soybean meal did not improve pig performance, but its addition to corn-soybean meal-based Phase III nursery diets improved gain:feed ratio and energy and AA digestibility.

Amino Acids↗

PubMed1986

Effects of hydrocortisone on carbohydrase concentrations, de novo synthesis and turnover patterns in immature rat intestine.

Hydrocortisone administration to infant rats enhanced cellobiase and maltase activities and induced precocious expression of sucrase and trehalase activities along the length of the small intestine. These activity changes reflected proportional concentration increases in the enzymes lactase (EC 3.2.1.23), maltase/glucoamylase (EC 3.2.1.20) and sucrase-isomaltase (EC 3.2.1.48/10). Administration of an equivalent tracer dose of [3H]leucine (by body weight) to control and hydrocortisone-treated infant rats resulted in greater accumulation of label in the carbohydrase pools of the treated rats, suggesting their increased de novo synthesis. The increased concentrations of lactase and maltase/glucoamylase induced by exogenous hydrocortisone were matched by the presence of corresponding greater amounts of label in their brush border pools. Accumulation of label in each of the lactase, maltase/glucoamylase and sucrase-isomaltase pools was generally similar in the hydrocortisone-treated rats, suggesting equivalent stimulation of their synthesis as a group by the humoral agent. The turnover rates of the carbohydrases as a group were found to be similar and did not appear to differ in control and hydrocortisone-treated rats. Total protein synthesis rates were slightly greater in the intestine of the hydrocortisone-treated group of rats.

Aging↗

PubMed1984

Adaptation of the activity of membrane carbohydrases of chick small intestine to various carbohydrates.

Adaptation changes in membrane carbohydrases and those localized in the apical glycocalyx of enterocytes have been studied in chicks under the impact of carbohydrates. The investigated enzymes were not equally adapted to the carbohydrates of various degrees of polymerization. The response character of membrane carbohydrases depends on proximo-distal localization of enzymes in the small intestine and it is not specific to carbohydrates.

Adaptation, Biological↗

PubMed1977

Scope and mechanism of carbohydrase action: stereospecific hydration of D-glucal catalyzed by alpha- and beta-glucosidase.

A unique demonstration is presented of the capacity of glycosidases to create anomeric configuration de novo. Purifed Candida tropicalis alpha-glucosidase and sweet almond beta-glucosidase have been found to attack the same substrate, D-glucal, and to convert this unusual glycosyl substrate (which lacks alpha or beta anomeric configuration) to 2-deoxy-alpha-(or beta-) D-glucose, respectively. The stereospecificity of the hydration reaction catalyzed by each enzyme in D2O was revealed by the use of high-resolution (270 MHz) 1H magnetic resonance spectroscopy. The alpha-glucosidase caused a specific axial protonation (deuteration) of D-glucal at C-2, and formation of 2-deoxy-alpha-D-[2(a)-2H]glucose. The beta-glucosidase catalyzed an oppositely directed axial protonation at C-2 and formation of 2-deoxy-beta-D-[2(e)-2H]glucose. These results are not accounted for by the generally accepted mechanisms of carbohydrase action derived from studies with glycosidically linked substrates alone. D-Glucal apparently binds to the enzymes with essentially the same overall orientation as the D-glucosyl moiety of glycosidically linked substrates (with the double bond of D-glucal lying essentially in the plane of the similarly bound D-glucosyl group). Thus, the alpha-glucosidase evidently protonates D-glucal from above the double bond and alpha-D-glucosidic substrates from below the glycosidic oxygen; beta-glucosidase apparently protonates D-glucal from below the double bond and beta-D-glucosides from above the glycosidic oxygen. A detailed mechanism is proposed for the hydration of D-glucal by each enzyme, involving an incipient glycosyl carbonium ion and assuming the presence at the active site of two carboxyl groups arranged to account for catalysis of glycosylations from glycosidically linked substrates. That D-glucal serves as a glycosyl substrate for these enzymes strongly supports the concept that glycosidases and glycosyltransferases are catalysts of glycosylation (i.e., glycosylases), since this concept does not make the usual assumption that carbohydrases are restricted to acting on substrates having a glycosidic bond and either alph- or beta-anomeric configuration.

Candida↗

PubMed1968

Carbohydrase activities in the bovine digestive tract.

1. The carbohydrase activities of homogenates of mucosa from the abomasum, small intestine, caecum and colon, and of the pancreas of cattle were studied. 2. The disaccharidase activities were located mainly in the small intestine and showed a non-uniform pattern of distribution along the small intestine; trehalase activity was highest in the proximal part, lactase and cellobiase activities were highest in the proximal and middle parts and maltase activity was highest in the distal part. 3. The intestinal lactase and cellobiase activities were highest in the young calf and decreased with age, whereas the intestinal maltase and trehalase activities, which were very low compared with the lactase activity, did not change with age. 4. No intestinal sucrase or palatinase activity was detected in the calf or in the adult cow. 5. Homogenates of intestinal mucosa also exhibited amylase and dextranase activity. 6. Homogenates of the pancreas possessed a strong amylase activity and a weak maltase activity. The maltase activity did not change with age, whereas the amylase activity increased with age. 7. No marked differences were observed between the carbohydrase activities of calves fed solely on milk and those of calves given a concentrate-hay diet from 6 weeks of age.

Abomasum↗

PubMed1991

Synthesis and accumulation of protein and carbohydrases along the rat villus column.

Enterocytes of the intestinal mucosa of infant and adult rats continuously proliferate in the crypt, mature as they migrate along the villus column, and are discharged from the villus tip. We examined the synthesis patterns of total protein, lactase-phlorizin hydrolase, sucrase-isomaltase, and maltase-glucoamylase as well as the accumulation of these enzymes in cells during migration along the villus. Labeled leucine was administered intraperitoneally to suckling and young adult rats, and radioactivity was determined in protein and digestive carbohydrase pools of developing villus cells separated sequentially from tip to base of the villus column. The developing cells were found to continuously accumulate protein and carbohydrates as they ascended the villus column. In addition, incorporation of radioactivity into total protein and carbohydrase pools occurred at generally constant rates along the length of the villus. These studies showed that the differentiated enterocyte of both infant and young adult rat intestine exhibits a pattern of continuous growth while migrating the length of the villus column and maintains synthesis of protein and digestive carbohydrates at generally constant rates during this time.

Animals↗

PubMed1985

Nature of elevated rat intestinal carbohydrase activities after high-carbohydrate diet feeding.

Adult rats that were maintained on a low-carbohydrate intake showed rapid increase in the activities of sucrase, maltase, and lactase along the length of the small intestine when they were fed a high-starch diet. In the present study, we have identified these activity increases, and showed that they reflect proportional accumulations in enzyme-protein of sucrase-isomaltase (EC 3.2.1.10, 3.2.1.48), maltase-glucoamylase (EC 3.2.1.20), and neutral lactase (EC 3.2.1.23). It was determined that each of these enzymes exists in adult rat intestine in single immunoreactive form and accounts as a group for all sucrase, cellobiase, and most maltase and lactase activities. Dietary change from low to high carbohydrate (starch) resulted in an increase in [3H]leucine accumulation in each of the enzymes, without a change in the amount of label accumulation in total intestinal proteins. The increase in label accumulation in the brush-border carbohydrase pools was matched generally by proportional elevation in the pool concentrations of sucrase-isomaltase and lactase but not maltase. These studies suggest that the elevation of intestinal carbohydrase concentrations induced by high-carbohydrate feeding may involve selective stimulation of their synthesis.

Animals↗

PubMedDate not supplied

[The dynamics of carbohydrase desorption from the surface of the intestines in fish and in their parasitizing cestodes].

Data are obtained on the fixation strength of carbohydrases on the structures of digestive-absorptive surfaces of cestodes and intestines of their fish hosts. A dependence of the parasite's digestive activity on the activity of the host's enzymes has been established. General regularities of desorption dynamics of carbohydrases in studied animals and their specific peculiarities are noted.

Animals↗

PubMedDate not supplied

[Effect of amizil on the carbohydrase activity in intact animals and animals subjected to stress exposure].

Effect of a central cholinolytic drug amizyl on the activity of some digestive enzymes involved in carbohydrate hydrolysis was studied in experiments on control rats and animals exposed to immobilization stress. The experiments showed that amizyl administration modifies the activity of carbohydrases that could affect disintegration and assimilation of carbohydrases. Preliminary administration of the drug was shown to prevent substantially the changes in the enzyme activity occurring during stress situation.

Adrenocorticotropic Hormone↗

PubMed1984

Carbohydrases and their role in the biology of pathogenic fungi.

Pathogenic fungi form different carbohydrases belonging to exo- and endo-types mostly. There is a wider range of glycanases of pathogenic and facultatively pathogenic fungi which are capable of living in the free nature. The role of carbohydrases as aggressive factors of the corresponding agents of mycotic processes is increasing under a pronounced disbalance of carbohydrates in macroorganisms.

Carbohydrate Conformation↗