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Effect of alpha-amylase from fungi and bacteria on extending bread freshness was compared to this of scalded flour. The dough prepared by using Bulk Fermentation Process was supplemented with bacterial and fungal amylases or scalded flour. After baking and cooling loaf volume was measured and bread mechanical properties were estimated using a texture analyser. Texture studies were then repeated after 1, 3, 4 and 7 days. The obtained results show the relation between dosage of enzyme or scalded flour and bread volume as well as the rate of bread staling. Source of enzyme was found important, because bacterial alpha-amylase lowered bread quality, while fungal alpha-amylase extended shelflife not showing detrimental effects. Replacement of 2-6% of flour with scalded flour improved bread volume and retarded crumb firming. The influence on bread was similar to fungal alpha-amylase. The results prove that substitution of fungal α-amylase by scalded flour is possible. There is a need for such an exchange because in the last years many cases of asthma, induced by occupational exposure to alpha-amylase derived from Aspergillus oryzae, were reported.
α-Amylase has a wide range of applications in starch industries, i.e. baking, brewing, distillery, etc. The α-amylase production from Streptomyces erumpens MTCC 7317 immobilized cells was compared with that of free cells. The immobilized cells of S. erumpens in calcium alginate beads were more effective for production of α-amylase (12.2% more yield) than free cells. Response surface methodology (RSM) was used to evaluate the effect of main variables, i.e. incubation period, pH and temperature on enzyme production with immobilized cells. A full factorial Central Composite Design (CCD) was applied to study these main factors that affected α-amylase production. The experimental results showed that the optimum incubation period, pH and temperature were 36 h, 6.0 and 50°C, respectively for immobilized cells. Repeated batch fermentation of immobilized cells in shake flasks carried out in starch-beef extract medium showed that S. erumpens cells were physiologically active on the support even after four cycles of fermentation.
Production and purification of α-amylase by probiotic Lactobacillus plantarum MTCC 1407 has been investigated under submerged fennentation using Mann Rogassa Sharpe medium containing (1%) soluble starch in lieu of glucose (2%) as carbon source. Response Surface Methodology was used to evaluate the effect of main variables, i.e. incubation period, pH and temperature on enzyme production. A full factorial Central Composite Design was applied to study these main factors that affected α-amylase production. The experimental results showed that the optimum incubation period, pH and temperature were 36 h, 7.0 and 35°C, respectively. The purified enzyme (by ammonium sulphate precipitation) had a molecular mass of 75 450 Da in SDS-PAGE.
Activity of α-amylase in somatic muscles in different parts of the female body of Ascaris suum was examined. Highest activity was indicated for the head (31.38 u/mg) and the tail (22.98 u/mg). No statistically significant differences of enzyme activity were found between 1-1.5 cm segments into which the remaining part of worm’s body wall was divided. Total α-amylase activity in isolated muscles from the body wall situated posteriorly to the nematode’s vulva was higher than in the anterior part (p<0.05). Higher enzyme activity was also noted in dorsal muscles than in ventral.
The provenance of α-amylase from intestines of adult Ascaris suum was investigated by Ouchterlony method using sera of guinea pigs vaccinated with the enzyme protein extracted from the worm intestine or pig pancreas. No cross-reactivity was observed between sera raised against pig α-amylase and A. suum enzyme. The results support suggestions that α-amylase present in A. suum intestine is produced by the nematode and not required from the host intestine.
The tomato leaf miner, Tuta absoluta Meyrick (Lepidoptera: Gelechiidae), is one of the most destructive pest of solanaceae and it prefers tomato (Solanum lycopersicum L.). The aim of the current study was to investigate the effects of a wide range of seed proteinaceous extracts from different plant families against T. absoluta α-amylase activity. The effect of pH on the inhibitory activity of seed extracts showed that seed extracts of amaranth along with a wheat cultivar (Alvand, Aflak, Sarvdasht, Alborz, and Kavir) produced more than a 50% inhibition of the insect amylase. Aflak wheat seed extract at 10 μg, inhibited 81% of the insect amylase. This percent was the highest inhibition achieved. The other proteinaceous seed extracts had a lower effect on the enzymatic activity. Probit analysis showed that Aflak, Kavir, Alborz, Alvand, Sarvdasht, and amaranth inhibited the amylase activity with an I50 of 1.94, 3.24, 3.46, 3.31, 4.97, and 15.39 μg, respectively. The effect of pH on the inhibition of the α-amylase showed the highest inhibition of Amaranth and wheat, at a pH value of 8.0, which corresponds to the pH of the insect’s gut. Gel electrophoresis assays confirmed the spectrophotometric assays showing that the α-amylase of the insect gut was affected by the presence of the seed extracts. In the gel assay, a high concentration (14 μg protein) of amaranth proteinaceous seed extract greatly decreased the intensity of the α-amylase band. A high concentration of the Aflak wheat cultivar (10 μg protein) caused the disappearance of the amylase band in the gel. Thus, it is concluded that the physiochemical environment of the insect gut affects the interaction between digestive α-amylase and the metabolites. The experiments showed that seed proteinaceous extracts from non-host plant species, produced more inhibition of the insect amylase when compared to the host plant species. It appears that with evolution, adaptation took place so that insect/s could overcome the plant metabolites.
Five fungal isolates were screened for the production of α-amylase using both solid-state and submerged fermentations. The best amylase producer among them, Aspergillus niger JGI 24, was selected for enzyme production by solid-state fermentation (SSF) on wheat bran. Different carbon and nitrogen supplements were used to enhance enzyme production and maximum amount of enzyme was obtained when SSF was carried out with soluble starch and beef extract (1 % each) as supplements. Further attempts to enhance enzyme production by UV induced mutagenesis were carried out. Survival rate decreased with increase in duration of UV exposure. Partial purification of the enzyme using ammonium sulphate fractionation resulted in 1.49 fold increase in the enzyme activity. The enzyme showed a molecular weight of 43 kDa by SDS-PAGE. Metal ions Ca²⁺ and Co²⁺ increased the enzyme activity. The enzyme was optimally active at 30°C and pH 9.5.
This study assessed the effects of different doses of ethephon and gibberellin A3 on germination and α- and β-amylase activity in Amaranthus caudatus seeds exposed to different levels of salt stress. NaCl at 25 and 50 mM only delayed germination; at 75, 100 and 125 mM it caused 50%, 90% and 99.5% inhibition of Amaranthus caudatus seed germination. Both ethephon and GA3 (0.01, 0.1, 0.3 mM) effectively counteracted inhibition of seed germination under salinity. The stimulatory effect of ethephon appeared earlier, and the seeds were more sensitive to ethephon than to GA3. Ethephon enabled seed germination in the presence of all NaCl concentrations (75, 100, 125 mM) even after 24 h. GA3 alleviated inhibition caused by 75 and 100 mM NaCl until 48 h and did not affect reduction of germination caused by NaCl at 125 mM. NaCl (100 mM) reduced α- and β-amylase activity and seed germination after 14 h, and enhanced α-amylase activity after 20 h, although germination was reduced. Ethephon and GA3 increased α- but not β-amylase activity under salt stress during the first 14 h of incubation
 An organic solvent and surfactant stable α-amylase was obtained from soybean seeds. The direct and indirect effect of various organic solvents (non-polar, polar protic, and polar aprotic) and surfactants on the activity and stability of free enzyme was determined. The enzyme showed a very high catalytic efficiency and stabilization against most of the organic solvents and surfactants tested, except for few. Those organic solvents and surfactants (like chloroform, dimethyl formamide, n-butanol, and Tween 20), which caused an inhibition in enzyme activity, were used to study their effects on immobilized enzyme. The inhibitory effect was found to be decreased in immobilized enzyme as compared to free enzyme indicating that immobilization imparted stability to the enzyme. Moreover, the possibility of reuse of the enzyme in the presence of the organic solvents and surfactants was increased upon immobilization. The stability of soybean α-amylase towards organic solvents and surfactants shows that it is a potential candidate for use in organic-solvent biocatalysis as well as in detergent industries.
There has been an enormous interest in the development of alternative medicines for type 2 diabetes, specifically screening for phytochemicals with the ability to delay or prevent glucose absorption. The goal of the present study was to provide in vitroevidence for potential inhibition of α-glucosidase and α-amylase enzymes, followed by a confirmatory in vivostudy on rats to generate a stronger biochemical rationale for further studies on the ethanolic extract of Andrographis paniculata and andrographolide. The extract showed appreciable α-glucosidase inhibitory effect in a concentration-dependent manner (IC50=17.2±0.15 mg/ml) and a weak α-amylase inhibitory activity (IC50=50.9±0.17 mg/ml). Andrographolide demonstrated a similar (IC50=11.0±0.28 mg/ml) α-glucosidase and α-amylase inhibitory activity (IC50=11.3±0.29 mg/ml). The positive in vitroenzyme inhibition tests paved way for confirmatory in vivostudies. The in vivostudies demonstrated that A. Paniculata extract significantly (P<0.05) reduced peak blood glucose and area under curve in diabetic rats when challenged with oral administration of starch and sucrose. Further, andrographolide also caused a significant (P<0.05) reduction in peak blood glucose and area under the curve in diabetic rats. Hence α-glucosidase inhibition may possibly be one of the mechanisms for the A. paniculataextract to exert antidiabetic activity and indicates that AP extract can be considered as a potential candidate for the management of type 2 diabetes mellitus.
Kinetics of amylolytic hydrolysis of autoclaved and extruded potato starch using alpha-amylase and pullulanase mixtures were described. Maltodextrins with dextrose equivalent of 3, 5, 8 and 12 were obtained and their sugar compositions with HPLC method were analyzed. The low molecular sugar (PD 1-2) and oligosaccharide (PD 3-8) contents as well as relationship between dextrose equivalent of maltodextrins and oligosaccharide contents were determined.
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