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PubMed2001

Cooperativity and substrate specificity of an alkaline amylase and neopullulanase complex of Micrococcus halobius OR-1.

The saccharifying alkaline amylase and neopullulanase complex of Micrococcus halobius OR-1 hydrolyzes both alpha-(1,4)- and alpha-(1,6)-glycosidic linkages of different linear and branched polysaccharides. The following observations were made concerning the analysis of the coexpressed amylase and neopullulanase enzymes. Even though the enzymes were subjected to a rigorous purification protocol, the activities could not be separated, because both the enzymes were found to migrate in a single peak. By contrast, two independent bands of amylolytic activity at 70 kDa and pullulanolytic activity at 53 kDa were evident by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), reducing and nonreducing PAGE, and zymographic analysis on different polysaccharides. Preferential chemical modification of the enzyme and concomitant high-performance thin-layer chromatographic analyses of the saccharides liberated showed that amylase is sensitive to 1-(dimethylamino-propyl)-3-ethyl carbodiimide-HCl and cleaved alpha-(1,4) linkages of starch, amylose, and amylopectin producing predominantly maltotriose. On the other hand, formalin-sensitive neopullulanase acts on both alpha-(1,4) and alpha-(1,6) linkages of pullulan and starch with maltotriose and panose as major products. It is understood that neopullulanase exhibits dual activity and acts in synergy with amylase toward the hydrolysis of alpha-(1,4) linkages, thereby increasing the overall reaction rate; however, such a synergism is not seen in zymograms, in which the enzymes are physically separated during electrophoresis. It is presumed that SDS-protein intercalation dissociated the enzyme complex, without altering the individual active site architecture, with only the synergism lost. The optimum temperature and pH of amylase and neopullulanase were 60 degreesC and 8.0, respectively. The enzymes were found stable in high alkaline pH for 24 h. Therefore, the saccharifying alkaline amylase and neopullulanase of M. halobius OR-1 evolved from tapioca cultivar shows a highly active and unique enzyme complex with several valuable biochemical features.

Amylases↗
PubMed2004

Cloning of the thermostable alpha-amylase gene from Pyrococcus woesei in Escherichia coli: isolation and some properties of the enzyme.

Pyrococcus woesei (DSM 3773) alpha-amylase gene was cloned into pET21d(+) and pYTB2 plasmids, and the pET21d(+)alpha-amyl and pYTB2alpha-amyl vectors obtained were used for expression of thermostable alpha-amylase or fusion of alpha-amylase and intein in Escherichia coli BL21(DE3) or BL21(DE3)pLysS cells, respectively. As compared with other expression systems, the synthesis of alpha-amylase in fusion with intein in E. coli BL21(DE3)pLysS strain led to a lower level of inclusion bodies formation-they exhibit only 35% of total cell activity-and high productivity of the soluble enzyme form (195,000 U/L of the growth medium). The thermostable alpha-amylase can be purified free of most of the bacterial protein and released from fusion with intein by heat treatment at about 75 degrees C in the presence of thiol compounds. The recombinant enzyme has maximal activity at pH 5.6 and 95 degrees C. The half-life of this preparation in 0.05 M acetate buffer (pH 5.6) at 90 degrees C and 110 degrees C was 11 h and 3.5 h, respectively, and retained 24% of residual activity following incubation for 2 h at 120 degrees C. Maltose was the main end product of starch hydrolysis catalyzed by this alpha-amylase. However, small amounts of glucose and some residual unconverted oligosaccharides were also detected. Furthermore, this enzyme shows remarkable activity toward glycogen (49.9% of the value determined for starch hydrolysis) but not toward pullulan.

Cloning, Molecular↗
PubMed1991

Usefulness of peritoneal fluid amylase levels in the differential diagnosis of peritonitis in peritoneal dialysis patients.

Peritonitis continues to be a major cause of morbidity in peritoneal dialysis patients despite recent technological advances (Y systems) that have reduced peritonitis rates to much more acceptable levels. Most of the time when a peritoneal dialysis patient presents with peritonitis, it is infectious in origin. However, these patients occasionally develop other intra-abdominal pathology that requires more intensive medical care or, at times, surgical intervention. To help in the early differential diagnosis of the cause of peritonitis in these patients, peritoneal fluid amylase levels were prospectively obtained from 50 patients presenting to the hospital with peritonitis. Thirty-nine of them had typical infectious peritonitis, and their mean peritoneal fluid amylase level was 11.1 (range, 0 to 90). Six patients had pancreatitis and a mean peritoneal fluid amylase level of 550 U/L (range, 100 to 1,140 U/L). Five patients were found to have other intra-abdominal pathology, and their mean peritoneal fluid amylase level was 816 U/L (range, 142 to 1,746 U/L). In patients who did not respond to initial therapy, sequential peritoneal fluid amylase levels did not increase in patients with typical infectious peritonitis whereas it did increase in patients with other intra-abdominal pathology. In conclusion, it was found that peritoneal fluid amylase levels were helpful in the differential diagnosis of peritonitis in these patients. An elevated level (greater than 100 U/L) differentiated those patients with other intra-abdominal causes of peritonitis from those with typical infectious peritonitis.

Amylases↗
PubMed1983

Stimulation of amylase and sialic acid releases from dog submandibular gland slices by pilocarpine or high K+ medium: a possible role of calmodulin for their releases.

The mechanism of amylase and sialic acid releases stimulated by pilocarpine or high K+ medium was investigated in the slices of dog submandibular glands. The release of both amylase and sialic acid was dose-dependently increased by pilocarpine and a considerable release was observed at pilocarpine concentrations of more than 1 microM. Similar effects were observed when K+ concentration in the medium was increased and the maximal response was observed at 75 mM K+. The release of amylase and sialic acid by pilocarpine or K+ considerably decreased by removing Ca2+ from the medium and the slices. The release of amylase in the Ca2+-deficient slices was nearly recovered by the addition of 2.5 and 5.0 mM Ca2+, whereas that of sialic acid was recovered by only 60-75%. Ca2+ inhibitors, La3+ and verapamil, and calmodulin inhibitors, trifluoperazine, prenylamine, and W-7, significantly inhibited the release of amylase and sialic acid induced by the stimulants. These results suggest that the release of amylase and sialic acid stimulated by pilocarpine or K+ is dependent on the presence of Ca2+, and that the activation of calmodulin is involved in the process of the release.

Amylases↗
PubMed1989

The inhibitory effect of CR-1409 on amylase secretion and intracellular Ca2+ mobilization in rat pancreatic acini in vitro.

The inhibitory effects of CR-1409, a new glutaramic acid derivative developed as a cholecystokinin (CCK) receptor antagonist, on caerulein-stimulated amylase secretion and on intracellular Ca2+ ([Ca2+]i) mobilization were studied in isolated rat pancreatic acini. Pancreatic acini were prepared by collagenase digestion method and loaded with 1 microM fura-2/AM for measurement of the intracellular free Ca2+ concentration. Amylase release was examined by a perifusion method. Stimulation with 10(-10) M caerulein, 10(-5) M carbachol, or 10(-8) M gastrin-releasing peptide (GRP) led to biphasic amylase release and increase in [Ca2+]i. CR-1409 at 1 and 5 microM inhibited, by 50 and 84%, respectively, the amylase secretion and increase in [Ca2+]i induced by 10(-10) M caerulein, and 25 microM CR-1409 completely inhibited both amylase secretion and increase in [Ca2+]i induced by caerulein. However, 25 microM CR-1409 did not inhibit unstimulated secretion of amylase or the secretions induced by carbachol and GRP, which are also mediated by changes in intracellular Ca2+. We conclude that CR-1409 acts as a specific inhibitor of the CCK receptor in the pancreas, and is useful in studies on the involvement of the release and action of CCK in vitro.

Amylases↗
PubMed1990

Effects of treating corn silage with alpha-amylase and(or) sorbic acid on beef cattle growth and carcass characteristics.

The effects on beef cattle growth performance and carcass characteristics of feeding silages produced by altered fermentations were determined. Alpha-amylase was added at 0 or .05% (wet basis) and sorbic acid was added at 0 or .10% (wet basis) to chopped whole corn plants before ensiling in a 2 x 2 factorial arrangement of treatments. For three successive years, 40 beef heifers (224 kg) were fed these silages for 80 d, finished on corn-and-cob meal (107 d) and slaughtered when backfat thickness over the 13th rib reached 12 mm. Silages treated with alpha-amylase had a slightly higher percentage of N-free extract (P less than .10). Silages treated with sorbic acid had lower percentages of ADFN (P less than .10). During the silage-feeding phase, heifers fed silages treated with alpha-amylase gained more (P less than .01) daily than heifers fed the other two silages (.84 vs .78 kg) and they were more efficient (P less than .01) in weight gain per unit of dry feed consumed (.149 vs .139 kg). During the finishing phase, heifers that previously had been fed the alpha-amylase-treated silage continued to have higher (P less than .05) ADG (.93 vs .87 kg), although all were fed the same diet during this period. Added sorbic acid had no effect on ADG in either period. The percentage of kidney fat in heifers on the alpha-amylase treatments was increased (P less than .02, 2.2 vs 2.0). The biological mechanisms associated with the beneficial results of alpha-amylase addition are not understood yet.

Animal Feed↗
PubMed1996

Calibration of the Ektachem Amylase method using human reference materials and the Phadebas Blue Starch method as an interim reference method.

In a multilaboratory study a consensus was established to calibrate the Ektachem Amylase method to reproduce the results of the Phadebas Blue Starch method. The calibration graph has a slope = 3.39 and intercept = 25. For the Ektachem Amylase method the reaction-rate ratio between salivary and pancreatic amylase was calculated to be 0.89, relative to that of the Phadebas Blue Starch method. A calibration value for the Nordic Amylase Calibrator to be used on Ektachem analysers was determined to be close to 469 U l-1 for the current batch. However, since the difference from the stated value of 460 U l-1 is negligible, the authors recommend the use of the stated value for this and future batches of the Nordic Amylase Calibrator. An error of around 10% introduced by the presence of salivary amylase is comparable to the methods accepted by the Scandinavian Committee on Enzymes. Introduction of a consensus calibration reduced the interlaboratory variation by up to 40% at all levels.

Amylases↗
PubMed1985

The clinical significance of salivary amylase in duodenal aspirates in evaluation of exocrine pancreas function.

Salivary and pancreatic amylases in duodenal aspirates were quantitated in 419 consecutive tests performed on 378 patients suspected of having insufficiency of the exocrine pancreatic function. Salivary amylase was detected in samples from 31% of the tests. However, the amount of salivary amylase was sufficient to cause a misinterpretation in 13 tests only. Five of these tests originated from patients with a history of surgery for peptic ulcer disease. This group of patients tended to have large amounts of salivary amylase in the duodenal aspirates. In the unoperated patients (n = 336) 200 tests yielded values for the total amylase concentration above the lower level of the reference interval, and only in 8 of these tests (4%) did correction for salivary amylase change the results to values below the reference interval. It it concluded that quantitation of isoamylase activity in duodenal samples is unlikely to be of significant value in patients without a history of surgery for peptic ulcer disease.

Adult↗
PubMed1995

Stunting syndrome in broilers: effect of age and exogenous amylase and protease on performance, development of the digestive tract, digestive enzyme activity, and apparent digestibility.

Day-old male, meat-type chicks raised in brooder batteries were infected by orally administering an inoculum prepared from intestines of broiler chicks infected with stunting syndrome (SS). Naive controls were kept in a parallel room. The chicks were fed a commercial starter diet supplemented with two levels of enzyme preparations to 14 d of age. The experiment was continued to the age of 6 wk in order to estimate compensatory feed intake and growth. In a parallel study, digestibility of the feed was determined from 1 to 3 wk of age with control or inoculated chicks. The enzymes amylase and proteases were produced by Bacillus subtilis and Penicillium emersonii. Enzyme supplementation had no effect on feed intake, growth, or feed utilization, or on digestibility of fat, starch, protein, or energy. Because enzyme supplementation did not consistently affect performance of chicks and no interactions were observed between enzyme supplementation and infection status, data are presented for effects of infection only. Inoculation of SS-infective material reduced performance to 4 wk. Compensatory growth and feed intake were observed from the age of 4 wk onward. At the age of 6 wk the slight retardation of the inoculated chicks was not significant. On Week 1, retention of fat, starch, protein, and energy was significantly depressed in the inoculated chicks. At the age of 2 wk, retention of starch was not depressed, and at the age of 3 wk, the only consistent depression was that observed for fat. The proventriculus weight and content were consistently higher in inoculated chicks, as were the small intestine and intestinal content. The pH of the gizzard content was higher, and that of the small intestine content was lower, in the inoculated birds than in their control counterparts. Stunting syndrome infection was accompanied by a significant depression of trypsin activity in the pancreas at the age of 1 and 2 wk. At these periods, amylase and chymotrypsin were not affected. At 6 wk of age, the activities of amylase, trypsin, and chymotrypsin in the pancreas were higher in the inoculated than in the control birds. In the intestinal chime, amylase, trypsin, and chymotrypsin activities were lower in the inoculated birds on Week 1 and 2 (NS for amylase on Week 1). On Week 6, the activity of all enzymes assayed was higher in the inoculated birds (NS for amylase). It is suggested that the main factors depressing feed intake and growth in SS-infected birds are most probably beyond those of digestion.

Aging↗
PubMed1999

Purification and characterization of the heat-labile alpha-amylase secreted by the psychrophilic bacterium TAC 240B.

A total of 59 bacteria samples from Antarctic sea water were collected and screened for their ability to produce alpha-amylase. The highest activity was recorded from an isolate identified as an Alteromonas species. The purified alpha-amylase shows a molecular mass of about 50,000 Da and a pI of 5.2. The enzyme is stable from pH 7.5 to 9 and has a maximal activity at pH 7.5. Compared with other alpha-amylases from mesophiles and thermophiles, the "cold enzyme" displays a higher activity at low temperature and a lower stability at high temperature. The psychrophilic alpha-amylase requires both Cl- and Ca2+ for its amylolytic activity. Br- is also quite efficient as an allosteric effector. The comparison of the amino acid composition with those of other alpha-amylases from various organisms shows that the cold alpha-amylase has the lowest content in Arg and Pro residues. This could be involved in the principle used by the psychrophilic enzyme to adapt its molecular structure to the low temperature of the environment.

Amino Acid Sequence↗
PubMed2000

Total and pancreatic amylase measured with 2-chloro-4-nitrophenyl-4-O-beta-D-galactopyranosylmaltoside.

BACKGROUND: : Many different methods have been used to assay amylase activity, using nitrophenylated oligosaccharides as substrate; however, the hydrolysis steps in these methods are complex. METHODS: : We developed a new continuously monitoring assay for amylase activity in biological fluids, using 2-chloro-4-nitrophenyl-4-O-beta-D-galactopyranosylmaltoside (GalG2CNP) as the substrate; this assay was used with anti-human salivary amylase monoclonal antibodies for specific determination of the pancreatic isoenzyme. Amylase converted GalG2CNP into beta-D-galactopyranosylmaltose and 2-chloro-4-nitrophenol, which was measured at 405 nm. RESULTS: : GalG2CNP was cleaved between 2-chloro-4-nitrophenol and beta-D-galactopyranosylmaltose and did not undergo transfer reactions. The within-assay CVs (n = 20) for total amylase (T-AMY) and pancreatic amylase (P-AMY) were 0.6-1.6% and 0.5-2.5%, respectively; and day-to-day CVs (n = 10) for T-AMY and P-AMY were 0.8-3.7% and 0.6-4.1%, respectively. T-AMY and P-AMY activities in serum or urine obtained by the proposed method correlated well with those determined by the 2-chloro-4-nitrophenyl 4-O-beta-D-galactopyranosyl-beta-maltotetraoside method or the modified IFCC method. CONCLUSIONS: : This novel assay for T-AMY and P-AMY measures both activities stoichiometrically, directly, and easily, and may be suitable for routine procedures.

Amylases↗
PubMed2001

[Diagnostic significance of index alpha-amylase/glucose in amniotic fluid in prediction of fetal maturity].

An increase in alpha-amylase activity with parallel decrease in glucose concentration in amniotic fluid is observed during pregnancy. This interdependence is a theoretical basis for using an alpha-amylase/glucose index in fetal maturity evaluation. The aim of the study was to investigate usefulness of the alpha-amylase/glucose index in amniotic fluid in prenatal fetal maturity diagnosis. The study was carried out on 180 pregnant women, chosen by random selection, hospitalized in Polish Mother's Health Centre Hospital in the period from 15.06.1994 to 31.12.1995. 223 samples of amniotic fluid were tested for glucose concentration and alpha-amylase activity. It was found that the alpha-amylase/glucose < 6.0 index indicates a possibility of RDS occurring in neonates born before 72 hours of performed determination. The alpha-amylase/glucose > or = 6.0 index has high diagnostic value (95.8%) in prenatal prediction of fetal lung maturity.

Adult↗
PubMedDate not supplied

Measurement of alpha-amylase activity in white wheat flour, milled malt, and microbial enzyme preparations, using the Ceralpha assay: collaborative study.

This study was conducted to evaluate the method performance of a rapid procedure for the measurement of alpha-amylase activity in flours and microbial enzyme preparations. Samples were milled (if necessary) to pass a 0.5 mm sieve and then extracted with a buffer/salt solution, and the extracts were clarified and diluted. Aliquots of diluted extract (containing alpha-amylase) were incubated with substrate mixture under defined conditions of pH, temperature, and time. The substrate used was nonreducing end-blocked p-nitrophenyl maltoheptaoside (BPNPG7) in the presence of excess quantities of thermostable alpha-glucosidase. The blocking group in BPNPG7 prevents hydrolysis of this substrate by exo-acting enzymes such as amyloglucosidase, alpha-glucosidase, and beta-amylase. When the substrate is cleaved by endo-acting alpha-amylase, the nitrophenyl oligosaccharide is immediately and completely hydrolyzed to p-nitrophenol and free glucose by the excess quantities of alpha-glucosidase present in the substrate mixture. The reaction is terminated, and the phenolate color developed by the addition of an alkaline solution is measured at 400 nm. Amylase activity is expressed in terms of Ceralpha units; 1 unit is defined as the amount of enzyme required to release 1 micromol p-nitrophenyl (in the presence of excess quantities of alpha-glucosidase) in 1 min at 40 degrees C. In the present study, 15 laboratories analyzed 16 samples as blind duplicates. The analyzed samples were white wheat flour, white wheat flour to which fungal alpha-amylase had been added, milled malt, and fungal and bacterial enzyme preparations. Repeatability relative standard deviations ranged from 1.4 to 14.4%, and reproducibility relative standard deviations ranged from 5.0 to 16.7%.

Bacteria↗
PubMedDate not supplied

Prediction of pancreatic fistula by amylase levels of drainage fluid on the first day after pancreatectomy.

BACKGROUND/AIMS: We investigated whether it would be useful to monitor amylase levels of drainage fluid after pancreatic surgery for prediction of pancreatic fistula. METHODOLOGY: Twenty-six cases in which amylase levels of drainage fluid were determined after pancreatic surgery, were divided into 14 cases who did not develop pancreatic fistula and 12 cases who developed pancreatic fistula. Changes in amylase levels of sera and urine as well as drainage fluid were monitored. RESULTS: Amylase levels of drainage fluid were significantly higher in cases with pancreatic fistula than in cases without pancreatic fistula on the first postoperative day, but those levels in both groups decreased until the 7th postoperative day without significant difference. However, those levels in cases with pancreatic fistula significantly increased from the 9th postoperative day whereas the levels in cases without pancreatic fistula further decreased. There was no significant difference in amylase levels of sera or urine. CONCLUSIONS: Amylase levels of drainage fluid on the first postoperative day may be useful to predict development of pancreatic fistula and to plan appropriate management.

Aged↗
PubMed2000

[Prediction of peritoneal fluid pancreatic amylase to histopathological change and prognosis of acute experimental necrotic pancreatitis of monkey].

OBJECTIVE: To observe the significance of peritoneal fluid pancreatic amylase in predicting the degree of histopathological change and prognosis of acute necrotic pancreatitis (ANP) of monkey. METHODS: Injection of the mixture of bile and trypsin into the pancreatic duct set up ANP monkey model. RESULTS: The severity of ANP depended on the injection rate and volume, in correlation to the peritoneal fluid pancreatic amylase (PF Amylase) in the early stage of ANP. With the rate (3-13 ml/min) and volume (0.1-1.0 ml/kg) of injection increase, the PF Amylase in the early stage of the ANP significantly went up. Meanwhile, the survival time was negatively correlated to the PF Amylase in the early stage (0.5 hour) of ANP (t = -9.06 InX + 129.85, r = -0.88, P < 0.01). CONCLUSIONS: The PF Amylase in the early stage of ANP can effectively predict the severity of ANP and prognosis.

Amylases↗
PubMed2003

[A case of amylase-producing lung cancer].

A 72-year-old man was admitted to our hospital because of progressive dyspnea due to pulmonary emphysema. Chest CT revealed a nodular lesion in the right S6 and swollen right hilar lymph nodes. The diagnosis was not confirmed bronchoscopically. A subsequent biopsy of a subcutaneous mass in the left lateral pectoral region demonstrated metastatic cancer. Laboratory data on admission showed marked elevation of amylase activity in both serum and urine. Amylase isozyme patterns identified the salivary types. The pancreas and salivary glands were unlikely to have any clinical involvement in the hyperamylasemia, but lung cancer with subcutaneous metastasis was strongly suspected clinically as the source. Chemotherapy failed to prevent tumor progression and the patient eventually died of respiratory failure. Immunohistological examination of the subcutaneous lesion showed positive staining for salivary-type amylase, whereas that of the lung primary lesion disclosed small cell carcinoma and negative staining for amylase. In most cases, amylase-producing lung cancers have been diagnosed as adenocarcinoma. Amylase-producing small cell carcinoma is very rare.

Aged↗
PubMed2004

[Role of transforming growth factor beta3 on amylase secretion of submandibular gland cells in rat].

OBJECTIVE: To investigate the role of transforming growth factor beta3 (TGF-beta3) on the amylase secretion of rat submandibular gland cells (RSGCs). METHODS: The RSGCs were cultured and identified. The expressions of CK 8.13, S-100 and Vimentin in the RSGCs were examined by immunohistochemical staining. The experimental group was divided into 5 groups according to different concentrations of TGF-beta3 (0.5, 1.0, 5.0, 10.0 and 25.0 ng/ml) and no TGF-beta3 culture was used as control group. The effects of TGF-beta3 on the cell proliferation and amylase secretion were examined at the 24th, the 48th, the 72nd and the 96th hour. MTT colorimetric method was used to estimate vital force of culture cells. Amylase protein was assayed by auto-biochemistry equipment and Western blotting. RESULTS: The RSGCs were stained positively for CK 8.13 and S-100, but negatively for Vimentin. There were no significant differences in absorbency between the experimental groups and the control group (P>0.05). Compared with the control group, TGF-beta3 at concentrations of 0. 5-10. 0 ng/ml significantly stimulated the amylase secretion of RSGCs after 72 and 96 hours (P<0.01). But high concentration of TGF-beta3 (25.0 ng/ml) showed no stimulation. Western blotting demonstrated that the cultured RSGCs and submandibular gland had the same band of amylase electrophoresis. CONCLUSION: TGF-beta3 can stimulate RSGCs to differentiate and to secrete amylase, but TGF-beta3 has no effect on proliferation of RSGCs.

Amylases↗
PubMed2004

Bread eating induced oral angioedema due to alpha-amylase allergy.

Inhalation of dust from different enzymes can be the cause of occupational asthma in exposed workers. Enzymes from different sources are being increasingly used in food. Few cases of food allergy to alpha-amylase induced by eating bread have been reported. Those cases were reported in bakery-related patients and in a pharmaceutical-industry worker. A 25-year-old farmer suffered sneezing, rhinorrhea, oropharyngeal itching, hoarseness, cough, and non-wheezy dyspnea after eating white bread. Skin prick tests (SPT) with common aeroallergens and food allergens revealed only sensitization to Olea europaea pollen. SPT response was positive to Aspergillus oryzae alpha-amylase. Specific IgE against alpha-amylase was positive. A double-blind placebo-controlled challenge with 5 mg of uncooked -amylase induced sneezing, cough, oral angioedema within 10 minutes. The provocation test with 50 g of white bread gave similar findings. This case indicates that alpha-amylase contained in bread may provoke IgE-mediated food allergy. It is worth noting that in this case, the only source of alpha-amylases sensitization was bread.

Adult↗