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PubMed1991

The effect of concentration of tannin-rich bean hulls (Vicia faba L.) on activities of lipase (EC 3.1.1.3) and alpha-amylase (EC 3.2.1.1) in digesta and pancreas and on the digestion of lipid and starch by young chicks.

The effect of different concentrations of tannin-rich field-bean (Vicia faba L.) hulls at 0, 20, 50, 150 and 300 g/kg dietary inclusion on the activities of lipase (EC 3.1.1.3) and alpha-amylase (EC 3.2.1.1) in digesta and pancreas and on the digestion of lipid and starch was studied in 2-3-week-old male broiler chicks. Low dietary concentrations of tannins (20 and 50 g hulls/kg) enhanced the activity of lipase in digesta from both the jejunum and ileum, the 20 g hulls/kg effecting the greatest enhancement, but no stimulatory effect on the activity of digesta alpha-amylase was observed. High dietary concentrations of tannins (150 and 300 g hulls/kg) inhibited both lipase and alpha-amylase activities in digesta from both the jejunum and ileum, the 30 g hulls/kg causing the most inhibition. Tannins did not increase the activities of lipase or alpha-amylase in pancreatic homogenates, but at high concentrations (150 and 300 g hulls/kg) they lowered slightly the pancreatic activity of alpha-amylase. Nutrient digestion was less influenced by the concentration of tannins than digesta enzyme activities.

Animals↗
PubMed1995

Measurement of starch digestion of naturally 13C-enriched weaning foods, before and after partial digestion with amylase-rich flour, using a 13C breath test.

Malnutrition in infancy is a global problem which leads to retardation of childhood growth and development. There is a pressing need to improve weaning strategies for infants of the developing world. Traditional Gambian weaning foods are watery and of low energy density, but addition of energy in the form of fat and carbohydrate leads to thick, viscous gruels which are difficult to ingest. Partial digestion with amylase (EC 3.2.1.1)-rich flour reduces their viscosity while retaining their energy density. The aim of the present study was to measure the digestibility of a maize-based weaning food, before and after amylase digestion, in malnourished children using a 13C breath test. Ten children (aged 7-16 months; mean weight-for-age Z score -0.8) received isovolumetric and isoenergetic quantities of a maize-based weaning food naturally abundant with 13C. Breath samples were collected at intervals of 30 min for 5 h thereafter and 13CO2 enrichment was measured by isotope-ratio mass spectrometry. Percentage dose of 13C recovered increased from a mean 13.7 (SD 3.7)% before, to 18.3 (SD 5.6)% after ingestion of amylase-treated weaning foods (P < 0.1). There was a significant inverse relation between age and weight, and percentage dose of 13C recovered in children receiving amylase-treated feeds. There were no differences in concentrations of amylase in saliva of infants or breast milk of their mothers. Partial digestion of supplementary foods may improve the nutrition of undernourished weaning children, not only by reducing their viscosity, thereby increasing ingestion, but also by improving their digestion and thereby their absorption.

Age Factors↗
PubMed2003

Does the consumption of amylase-containing gruels impact on the energy intake and growth of Congolese infants?

OBJECTIVE: To assess the effect of the incorporation of amylase in maize-based flours prepared as gruels on the energy intake and growth of Congolese infants. DESIGN: A randomised controlled trial. At 18 weeks of age, infants were randomised into either an intervention group, where they were provided with a maize/soya-based flour that contained amylase, or a control group, where they were provided with a similar flour that did not contain amylase. SETTING: Urban borough of Poto-Poto in Brazzaville, The Congo. SUBJECTS: Eighty infants (40 in each group) were randomised into intervention and control groups. Three infants in the intervention group and two controls subsequently dropped out. RESULTS: At 24 weeks, the addition of amylase resulted in a significant increase in energy intake (in kJ kg-1 day-1) from gruels without affecting breast milk consumption. In contrast, total energy intake (in kJ kg-1 day-1) did not differ significantly between groups (P= 0.08). After adjustment for morbidity and previous growth, infants in the intervention group showed better growth in length during the trial (+0.22 cm month-1; P= 0.04), especially between 24 and 31 weeks of age (+0.51 cm month-1; P< 0.01). There were no differences in weight velocity between groups. CONCLUSIONS: The findings of this study suggest that the consumption of amylase-treated gruels allows an increase in energy intake from these gruels without affecting breast milk consumption but has no impact on total daily energy intake. However, if started after 6 months, it could be effective in preventing faltering of infant linear growth.

Amylases↗
PubMed1985

SCE Nordic alpha-amylase method selection and calibration study. A report by the Committee of Enzymes of the Scandinavian Society for Clinical Chemistry (SCE).

Seventy-six Nordic routine laboratories participated in a joint SCE-NORDKEM study comprising evaluation, selection, and temporary calibration of amylase methods. Human control materials with known fractions of salivary and pancreatic amylase were determined by seven routine amylase assays based on substrates with glucosyl (G) chain lengths G4, G5, G5-6, G7, G9, amylopectin and blue starch polymer (Phadebas). The data were plotted before and after calibration of each method using a human pancreatic calibrator with an assigned value of 390 U/l (37 degrees C, Phadebas). the study led to three conclusions: The analytical overestimation of salivary to pancreatic amylase ratio (S:P) increased with decreasing number of glucosyl units in the substrates. Relative to the S:P value of blue starch polymer (set at 1.00), for example, tetraose mean S:P value was 1.55. The hydrolysis rates relative to that with blue starch polymer decreased with the number of glucosyl units in the substrates. The precalibration values of all methods spread over an approximately six-fold range. Post-calibration values of all methods, except tetraose, showed an acceptable inter-laboratory comparability. The CV values for low, medium, and high controls were about 5.5, and 6% respectively. As a temporary solution to the current problem of diverse amylase assays, the SCE suggests calibration of the methods considered acceptable in this study. The long-term effects will be evaluated in a follow-up study within a year.

Calibration↗
PubMed1999

The effects of high-intensity intermittent exercise on saliva IgA, total protein and alpha-amylase.

The aim of this study was to assess the effect of an acute bout of high-intensity intermittent exercise on saliva IgA concentration and alpha-amylase activity, since this type of training is commonly incorporated into the training programmes of endurance athletes and games players. Eight well-trained male games players took part in the study. They reported to the laboratory after an overnight fast and performed a 60-min cycle exercise task consisting of twenty 1-min periods at 100% VO2max, each separated by 2 min recovery at 30% VO2max. Unstimulated whole saliva was collected over a 5-min period into pre-weighed tubes and analysed for total protein, saliva IgA and alpha-amylase. The saliva flow rate ranged from 0.08 to 1.40 ml x min(-1) at rest and was not significantly affected by the exercise. The performance of the intermittent exercise bout did not affect the saliva IgA concentration, but caused a five-fold increase in alpha-amylase activity (P<0.01 compared with pre-exercise) and a three-fold increase in total protein concentration (P<0.01). These returned to pre-exercise values within 2.5 h post-exercise. It has been suggested that IgA concentration should be expressed as the ratio to total protein concentration, to correct for any concentrating effect due to evaporative loss of saliva water when breathing through the mouth (as in strenuous exercise). The present study clearly demonstrates that this is not appropriate, since there is an increase in salivary protein secretion rate immediately after exercise (571+/-77 microg x min(-1) compared with 218+/-71 microg x min(-1) pre-exercise; P<0.05). The increased saliva alpha-amylase activity after exercise may improve the protective effect of saliva, since this enzyme is known to inhibit bacterial attachment to oral surfaces. The saliva alpha-amylase secretion rate was lower immediately pre-exercise than at any other instant, which may have been due to anticipatory psychological stress, although the subjects were all familiar with interval exercise. This emphasizes the need for true resting non-stressed control conditions in future studies of the effects of exercise on saliva constituents.

Adult↗
PubMed2005

Study of the inhibition of alpha-amylase by the benzo[c]phenanthridine alkaloids sanguinarine and chelerythrine.

Inhibition of porcine pancreas and human saliva alpha-amylase (EC 3.2.1.1) by sanguinarine and chelerythrine was studied. The inhibition of alpha-amylase was assayed using a biosensor method which utilises a flow system equipped with a peroxide electrode. 250 microM sanguinarine and 250 microM chelerythrine cause complete inhibition of 1.9 nkat alpha-amylase from porcine pancreas. The same concentration of sanguinarine and chelerythrine caused 23.9% and 7.5% inhibition, respectively, of 1.9 nkat alpha-amylase from human saliva. Mixed type and partially reversible inhibition was found for both alpha-amylases treated with either alkaloid.

Alkaloids↗
PubMed1978

Rapid amylase and lipase determinations by nephelometry.

The Coleman 91 nephelometer provides rapid, simple amylase and lipase assays, which are particularly suited to emergency requests. Linearity of amylase compares favorably with that of the Phadebas assay, and comparable precision was obtainable with serum and urine. Normal ranges for serum amylase are slightly higher than those based on the amyloclastic end-point assay. The serum lipase assay shows improved linearity over titrimetric procedures, although kinetics remain variably non-linear. Occasional sera show discordantly elevated nephelometric lipase and normal titrimetric lipase. Precision of the nephelometric lipase assay is somewhat lower than that of amylase; normal ranges are considerably higher than those based on titrimetry. Extremely lactescent sera may yield falsely low nephelometric amylase and lipase activities: these sera must be serially diluted to achieve actual values.

Amylases↗
PubMed2002

Postruminal administration of partially hydrolyzed starch and casein influences pancreatic alpha-amylase expression in calves.

The objective was to examine the effects of postruminal partially hydrolyzed starch (SH) and/or casein on the expression of pancreatic alpha-amylase mRNA, protein and activity in calves. Holstein calves [(n = 24) 88 plus minus 3 kg body weight (BW)], fitted with abomasal infusion cannulas, were randomly assigned within block (week of infusion) to one of four abomasal infusion treatments. Calves were fed an alfalfa-based diet, and SH [4 g/(kg BW.d)] and/or casein [0.6 g/(kg BW.d)] was infused abomasally for 10 d before tissue collection. There was a SH x casein interaction (P < 0.10) for pancreatic weight (g and g/kg BW) because casein increased pancreatic weight in the absence of SH but did not influence pancreatic weight in the presence of SH. Pancreatic alpha-amylase mRNA tended to be lower (P = 0.06) and protein and activity (U/g pancreas and U/g protein) were lower (P = 0.02) in calves receiving abomasal SH. The concentration of pancreatic trypsin activity (U/g pancreas and U/g protein) was lower (P < 0.03) in calves receiving abomasal SH. There was a SH x casein interaction for total alpha-amylase and trypsin activity [U/pancreas and U/(pancreas.kg BW)] because casein increased total activity in the absence of SH but not in the presence of SH. These data suggest that increases in small intestinal protein flow enhance pancreatic weight and thus total pancreatic alpha-amylase and trypsin activity, yet small intestinal SH inhibits the increase in pancreatic weight resulting from increased small intestinal protein flow. Additionally, postruminal SH decreases alpha-amylase expression largely by translational events.

Abomasum↗
PubMed1986

The alpha-amylase gene in Drosophila melanogaster: nucleotide sequence, gene structure and expression motifs.

We present the complete nucleotide sequence of a Drosophila alpha-amylase gene and its flanking regions, as determined by cDNA and genomic sequence analysis. This gene, unlike its mammalian counterparts, contains no introns. Nevertheless the insect and mammalian genes share extensive nucleotide similarity and the insect protein contains the four amino acid sequence blocks common to all alpha-amylases. In Drosophila melanogaster, there are two closely-linked copies of the alpha-amylase gene and they are divergently transcribed. In the 5'-regions of the two gene-copies we find high sequence divergence, yet the typical eukaryotic gene expression motifs have been maintained. The 5'-terminus of the alpha-amylase mRNA, as determined by primer extension analysis, maps to a characteristic Drosophila sequence motif. Additional conserved elements upstream of both genes may also be involved in amylase gene expression which is known to be under complex controls that include glucose repression.

Amino Acid Sequence↗
PubMed1994

alpha-Amylase hypersensitivity in non-exposed millers.

Occupational hypersensitivity to alpha-amylase among bakers and workers in the pharmaceutical industry has been described. We present the results of skin tests and in vitro methods used to assess alpha-amylase sensitivity in 259 millers. There was no occupational contact with the enzyme in this population. Positive skin tests to this allergen were obtained in 16 subjects (6.18 per cent), specific IgE values were found in seven subjects (2.7 per cent), specific IgG was detected on 45 workers (17.37 per cent) and high values for IgG (> 2.5 absorbance units) were found in 12 subjects (4.63 per cent). Furthermore, specific IgE and IgG could be determined in several sera by immunoblotting. All these facts suggested that millers were sensitized to Aspergillus oryzae alpha-amylase, although the allergen was not used by these workers. A cross-reaction cannot be excluded; however, it is the authors' opinion that wheat or wheat flour is a natural substrate for fungi and that the moulds that grow on cereals or cereal-derived by-products need to secrete amylases to support their own development. Hence the workers may be indirectly sensitized to amylases.

Aspergillus oryzae↗
PubMed1990

Processing of an NH2-terminally extended thermostable alpha-amylase by Bacillus subtilis alkaline protease.

To analyze the processing of extracellular enzymes of Bacillus subtilis, an NH2-terminally extended hybrid alpha-amylase [pTUBE638-alpha-amylase (E24)] was purified from the periplasm of E. coli(pTUBE638) as the substrate for the in vitro processing reaction, in which a 21-amino-acid extra-peptide was added at the NH2-terminus of the mature thermostable alpha-amylase. The extended peptide in pTUBE638-alpha-amylase (E24) was completely processed by the extracellular alkaline protease of B. subtilis alone at pH 7.5 to 10.0. The processing was inhibited by 2 mM PMSF. In contrast, the neutral protease did not process the extended peptide. The processing activity of the purified alkaline protease was fully active in 100 mM phosphate and glycine-NaCl-NaOH buffer while it was partially active in 100 mM Tris-HCl or MOPS buffer. The optimum pH of the activity ranged from 8.0 to 9.0, although the optimum pH of the alkaline protease activity toward casein and Azocoll was 10.5. The NH2-terminal amino acid sequences of the enzymes processed in vitro coincided with those of the mature extracellular thermostable alpha-amylases in the culture medium of B. subtilis (pTUBE638). The appearance of the processing activity of alkaline protease was correlated with the changes of the pH in the culture medium.

Amino Acid Sequence↗
PubMed1991

Substrate-selective activation of histidine-modified porcine pancreatic alpha-amylase by chloride ion.

Porcine pancreatic alpha-amylase (1,4-alpha-D-glucan glucanohydrolase) [EC 3.2.1.1] has both amylase activity (hydrolysis of alpha-1,4-D-glucoside bond of starch) and maltosidase activity (hydrolysis of p-nitrophenyl-alpha-D-maltoside to p-nitrophenol and maltose). By the modification of histidine residues of porcine pancreatic alpha-amylase with diethylpyrocarbonate (DEP), both amylase and maltosidase activities were decreased in the absence of chloride ion. In the presence of chloride ion, however, maltosidase activity of the modified enzyme was increased to more than 260% of that of the native enzyme, whereas amylase activity was decreased to less than 15% of the native enzyme. Since the chloride ion binding site is part of the active site loop [Buisson et al. (1987) Food Hydrocolloids 1,399-406 and Buisson et al. (1987) EMBO J. 6, 3909-3916], the special arrangements of both catalytic and modified histidine residues induced by the chloride ion binding would enhance only the maltosidase activity of the histidine-modified enzyme.

Animals↗
PubMed1985

Preparation of non-reducing-end substituted p-nitrophenyl alpha-maltopentaoside (FG5P) as a substrate for a coupled enzymatic assay for alpha-amylases.

p-Nitrophenyl O-6-deoxy-6-[(2-pyridyl)amino]-alpha-D-glucopyranosyl-(1----4)-O-alpha-D - glucopyranosyl-(1----4)-O-alpha-D-glucopyranosyl-(1----4)-O-alpha-D- glucopyranosyl-(1----4)-alpha-D-glucopyranoside, FG5P, was prepared, taking advantage of the action of Bacillus macerans cyclodextrin glucanotransferase on a mixture of O-6-deoxy-6-[(2-pyridyl)-amino]-alpha-D-glucopyranosyl-(1----4)-O-alpha- D- glucopyranosyl-(1----4)-O-alpha-D-glucopyranosyl-(1----4)-O-alpha-D- glucopyranosyl-(1----4)-O-alpha-D-glucopyranosyl-(1----4)-D-glucose and p-nitrophenyl alpha-glucoside. The maltopentaose derivative is resistant to alpha-glucosidase and is suitable as a substrate for the alpha-amylase assay coupled with alpha-glucosidase in which the activity of alpha-amylase is determined by measuring the amount of p-nitrophenol liberated by alpha-glucosidase from p-nitrophenyl alpha-glucoside and p-nitrophenyl alpha-maltoside produced by the action of alpha-amylase. This alpha-amylase assay method was applied for determination of alpha-amylases in human serum.

Bacillus↗
PubMed1986

Two tandemly located promoters, artificially constructed, are active in a Bacillus subtilis alpha-amylase secretion vector.

An 85 bp DNA fragment, the nucleotide sequence of which had 84% homology with the sequence for the promoter, ribosome binding site and NH2-terminal five amino acids of the Bacillus amyloliquefaciens alpha-amylase gene, was chemically synthesized. In order to analyze the promoter activity of a Bacillus subtilis alpha-amylase secretion vector, the fragment was inserted between the promoter and signal peptide-coding region of Bacillus subtilis alpha-amylase gene. Both promoters, tandemly repeated, functioned in transcribing the B. subtilis alpha-amylase signal peptide-coding region followed by the Escherichia coli beta-lactamase structural gene. The transcription initiation sites were determined by the primer extension method. The extracellular production of beta-lactamase was stimulated by two promoters as compared with that by the plasmids containing either promoter region alone. The change of two amino acids in the NH2-terminal region of the B. subtilis alpha-amylase signal peptide had no effect on the secretion of beta-lactamase from B. subtilis cells.

Bacillus subtilis↗
PubMed1994

C-terminal truncations of a thermostable Bacillus stearothermophilus alpha-amylase.

A series of truncated proteins from a thermostable Bacillus stearothermophilus alpha-amylase was prepared to study the importance of the extension in the C-terminus compared with other liquefying Bacillus alpha-amylases. The mutations introducing new translation termination sites shortened the 515 amino acid residue-long wild type enzyme by 17, 32, 47, 73 or 93 residues. The longer the truncation, the lower the specific activity of the enzyme. Only the two longest mutant proteins were active: the specific activity of the 498 residue variant was 97% and protein 483 was 36% that of the parental enzyme. The Km values of starch hydrolysis changed from 1.09 for wild type enzyme to 0.35 and 0.21 for mutants 498 and 483, respectively, indicating altered substrate binding. The mutant enzymes had almost identical pH and temperature optima with the wild type amylase, but enhanced thermal stability and altered end product profile. The consequences of the truncation to the structure and function of the enzymes were explored with molecular modeling. The liquefying amylases seem to require approximately 480 residues to be active, whereas the C-terminal end of B.stearothermophilus amylase is required for increased activity.

Amino Acid Sequence↗
PubMed1988

Serum amylase and macroamylase in patients with systemic lupus erythematosus.

We measured serum amylase and macroamylase activity in 25 patients with systemic lupus erythematosus (SLE) and 15 controls. The mean (+/- SD) for SLE was greater than for the controls (161 +/- 71.8 versus 116 +/- 38.8 units/dl). Five patients (20%) had elevated amylase and 6 (25%) had a macroamylase present. None of the controls had amylase elevation or macroamylase. None of the patients had abdominal pain and there was no observable correlation of amylase activity with disease activity, drugs, or renal function. Elevation of serum amylase in SLE without pancreatitis is frequent, as is the presence of macroamylase. Autoantibodies to this serum enzyme may be frequent in SLE.

Amylases↗
PubMed1976

Amylase--its clinical significance: a review of the literature.

This review of the English literature on amylase was undertaken because no recent discussion of the subject could be located, no comprehensive list of disorders causing hyperamylasemia or hyperamylasuria is available, and several major advances in the area have been made, notably the amylase isoenzyme determination and Cam/Ccr ratio. Several important concepts have emerged from this review. First, hyperamylasemia and hyperamylasuria are not specific indices of the presence of pancreatic disease or damage. Second, serum and urinary amylase levels can be spuriously normal with hypertriglyceridemia and pancreatitis. Third, the current emphasis on diagnostic methods for measuring serum amylase isoenzymes promises to improve the specificity of this determination. It will also enhance our understanding of the sources, distribution, metabolism, and elmination of amylase. Fourth, the development of the Cam/Ccr ratio may provide a practical diagnostic tool for separating clinically significant hyperamylasemia due to pancreatitis from that caused by other factors. Both the the isoamylase determination and Cam/Ccr ratio clearly require future research to place their clinical application in the proper perspective.

Amylases↗
PubMed1988

Effects of verapamil on amylase release from rat pancreatic acini and its relation to calcium fluxes.

The effects of verapamil on amylase release and Ca2+ fluxes from rat pancreatic acini have been studied. Verapamil at concentrations above 10 microM dose-dependently inhibited amylase release stimulated by carbachol, but enhanced the amylase release stimulated by cholecystokinin (CCK) and secretin. Verapamil had no significant effect on calcium uptake induced by carbachol or CCK, but significantly inhibited Ca+2 efflux caused by carbachol and slightly increased that caused by CCK. In a Ca2+-free, EDTA-containing medium, the increase in cytoplasmic free Ca2+ caused by carbachol was significantly inhibited by verapamil. Verapamil alone up to 400 microM had no effect on the release of lactic dehydrogenase. In conclusion, the effect of verapamil on amylase release from rat pancreatic acini differs depending on the type of secretagogue used to stimulate amylase release. This effect is not related to blockage of Ca2+ uptake, indicating another mechanism of verapamil on pancreatic acini.

Amylases↗