scholarly journals Factors responsible for production of amylases from Aspergillus fumigatus Fresenius

2013 ◽  
pp. 11-20 ◽  
Author(s):  
Munira Akhter ◽  
Md Towhid Hossain ◽  
MN Anwar
Keyword(s):  
Enzyme Activity ◽  
Aspergillus Fumigatus ◽  
Ammonium Nitrate ◽  
Amylase Activity ◽  
Soluble Starch ◽  
Culture Ph ◽  
Enzyme Substrate ◽  
Amylase Production ◽  
Initial Culture

Aspergillus fumigatus Fresenius showed maximum amylase production at 27°C with an initial culture pH of the medium 6.0 after 72 h. of incubation. One per cent soluble starch and 0.15% ammonium nitrate in the medium supported the highest amylase activity. During enzyme-substrate reaction maximum enzyme activity was observed at 50°C and pH 4.0 with 2% starch. DOI: http://dx.doi.org/10.3329/cujbs.v3i1.13402 The Chittagong Univ. J. B. Sci.,Vol. 3(1&2):11-20, 2008

Statistical Analysis of Growth and Amylase Production by Aspergillus flavus grown on Different Carbon Sources

2013 ◽  
Vol 2 (1) ◽  
Author(s):  
M O Oyewale
Keyword(s):  
Carbon Source ◽  
Aspergillus Flavus ◽  
Amylase Activity ◽  
Carbon Sources ◽  
Dry Weight ◽  
Soluble Starch ◽  
Optimum Growth ◽  
Amylase Production ◽  
Level Of Significance ◽  
Cassava Peel

The mycelial dry weight and dinitrosalicylic acid (D.N.S.A.) method was used to determine growth and amylase production by Aspergillus flavus grown on different carbon sources. Growth of the fungus was determined at 24 h intervals over a period of six days by the dry mycelial weight methods, while the amylase activity in the culture filtrates of A. flavus was determined by the D.N.S.A method. A total of 45 samples were prepared to determine growth and amylase activity of Aspergillus flavus grown on different carbon sources. The concentration of the various carbon sources ranges between 0.4 to 2% W/V. Duncan’s multiple range test was used to determine the level of significance of the different carbon sources for effective growth and amylase production by Aspergillus flavus. Aspergillus flavus demonstrated the capability to produce significant growth and amylase activities in the medium containing soluble starch, sorghum and cassava peel as sole carbon source. The amount of mycelial dry weight produced from soluble starch, sorghum and cassava peel is significantly higher than those produced from other carbon sources. The data revealed that there is a correlation between growth and amylase production by Aspergillus flavus. The available data from this study showed that soluble starch is the best carbon source for optimum growth and amylase production by A flavus while sorghum and cassava peel are close substitute for optimum growth and amylase production by Aspergillus flavus. Keywords: Growth, amylase activity and Aspergillus flavus

scholarly journals 307 Characterization of Amylolytic Activities of Tulip Bulb Scales

HortScience ◽  
1999 ◽  
Vol 34 (3) ◽  
pp. 495D-495
Author(s):  
Anil P. Ranwala ◽  
William B. Miller
Keyword(s):  
Enzyme Activity ◽  
Amylase Activity ◽  
Gel Filtration ◽  
Soluble Starch ◽  
Degree Of Polymerization ◽  
Exchange Chromatography ◽  
Product Analysis ◽  
Ph Optimum ◽  
Tulip Bulb ◽  
Tulipa Gesneriana

Amylolytic activities extracted from scales of tulip (Tulipa gesneriana L. cv. Apeldoorn) bulbs stored at 4 °C for 6 weeks under moist conditions were characterized. Anion exchange chromatography of enzyme extract on DEAE-Sephacel revealed three peaks of amylolytic activity. Three enzymes showed different electrophoretic mobilties on nondenaturing polyacrylamide gels. The most abundant amylase activity was purified extensively with phenyl-agarose chromatography, gel filtration on Sephacryl S-200, and chromatofocusing on polybuffer exchanger PBE 94. The purified amylase was determined to be an endoamylase based on substrate specificity and end product analysis. The enzyme had a pH optimum of 6.0 and a temperature optimum of 55 °C when soluble starch was used as the substrate. The apparent Km value for soluble starch was 1.28 mg/ml. The inclusion of 2 mM CaCl2 in the reaction mixture resulted in a 1.4-fold increase in the enzyme activity. The presence of calcium ions also enhanced the thermo-stability of the enzyme at higher temperatures. The enzyme was able to hydrolyze soluble starch, amylose, amylopectin, and beta-limit dextrin, but it had no activity against pullulan, inulin, maltose, or p-nitrophenyl alpha-glucopyranoside. Only maltooligosaccharides, having a degree of polymerization of 7 or more, were hydrolyzed to a significant extent by the enzyme. Exhaustive hydrolysis of soluble starch with the enzyme yielded a mixture of maltose and matlooligosaccharides. This amylase activity was not inhibited by alpha- or beta-cyclodextrin upto a concentration of 10 mM. Maltose at a 50 mM concentration partially inhibited the enzyme activity, whereas glucose had no effect at that concentration.

scholarly journals Aktivitas Enzim Amilase Isolat Bakteri Amilolitik dari Tepung Sagu Basah dan Lingkungan Tempat Penyediaannya Secara Tradisional di Jayapura

2018 ◽  
Vol 6 (2) ◽  
pp. 47-52
Author(s):  
Suprapto Surapto ◽  
Tri Gunaedi ◽  
Basa T. Rumahorbo
Keyword(s):  
Enzyme Activity ◽  
Agar Medium ◽  
Amylase Activity ◽  
Soluble Starch ◽  
Bacterial Isolates ◽  
Clear Zone ◽  
Plate Method ◽  
Crude Enzyme Extract ◽  
Nutrient Agar Medium ◽  
Bacillus Subtilis Atcc

The study about the activity of the enzyme amylase from amylolytic bacterial isolates from wet sagoo starch and  its traditional provision environment had been done in Jayapura. The purposes of this study were to determine the activity of amylase enzyme and to identify the bacteria isolated from wet sagoo starch and its processing environment in Jayapura district. The method used was an experimental laboratorium in which isolation of amylolytic bacteria was performed by using nutrient agar medium with 1% soluble starch on spreed pour plate method. The enzyme activity was detected with 0.2% iodine in 2% potassium iodide which were able to form a clear zone. The protein content of the crude enzyme extract was determined by the Bradford method using bovine serum albumin (BSA). Amylase enzyme activity was determined by the formula: DUN/ml = [(R0-R1)/R0] [dilution factor] DUN/ml (dextrinizing units per ml). The results showed that there were 15 isolates amylolytic bacteria. Four (4) bacterial isolates have amylolytic power of more than 30 mm. The amilase activity of amylolytic bacterial of all  isolates were quite high: which were 35 577, 18 903,  32 106 and 46 600 U/mg for SU4, SU13, SU23 and SU40 respectively. The identification of isolates indicated that the three isolates are members of the Bacillus cereus ATCC 14 579 types with a similarity value of 71.70% to 81.10%, and one isolate is Bacillus subtilis ATCC 6501 members with a similarity value of 94.30%. Keywords: Amylolytic bacteria, amylase activity, characterization, sago flour.

scholarly journals Production of Fungal Amylases Using Cheap, Readily Available Agriresidues, for Potential Application in Textile Industry

2014 ◽  
Vol 2014 ◽  
pp. 1-9 ◽  
Author(s):  
Shalini Singh ◽  
Sanamdeep Singh ◽  
Vrinda Bali ◽  
Lovleen Sharma ◽  
Jyoti Mangla
Keyword(s):  
Aspergillus Fumigatus ◽  
Textile Industry ◽  
Amylase Activity ◽  
Test Strain ◽  
Pomegranate Peel ◽  
Nutrient Salt ◽  
Amylase Production ◽  
Wet Processing ◽  
Initial Ph

The study aimed at isolation and screening of fungal amylase producer, optimization of solid state fermentation conditions for maximum amylase production by the best amylase producer, and characterization of the crude amylases, so produced.Aspergillus fumigatusNTCC1222 showed the highest amylase activity (164.1 U/mL) in secondary screening under SSF conditions and was selected for further studies. The test strain showed maximum amylase production (341.7 U/mL) and supernatant protein concentration (9.7 mg/mL) for incubation period (6 days), temperature (35°C), initial pH (6.0), nutrient salt solution as moistening agent, and beef extract as nitrogen source. Pomegranate peel produced maximum amylase activity, but wheat bran (only slightly lesser amylase activity as compared to that of pomegranate peel) was chosen for further studies, keeping in mind the seasonal availability of pomegranate peel. TLC confirmed the amylase produced to beα-type and 60 kDa was the molecular weight of the partially purified amylase. The enzyme showed maximum enzyme activity at pH 6.0, temperature of 55°C, and incubation time of 60 minutes. UV (616.0 U/mL) and chemical (814.2 U/mL) mutation enhanced amylase activity as compared to wild test strain. The study indicates thatAspergillus fumigatusNTCC1222 can be an important source of amylase and the crude enzyme, hence obtained, can be cost effectively applied in multiple sections of textile wet processing.

scholarly journals High Amylase Production by a Novel Strain of Bacillus amyloliquefaciens M37 Isolated from Can Gio Mangrove Forest, Vietnam

2021 ◽  
Vol 12 (4) ◽  
pp. 4675-4685
Keyword(s):  
Bacillus Amyloliquefaciens ◽  
Mangrove Forest ◽  
Amylase Activity ◽  
Carbon Sources ◽  
Soluble Starch ◽  
Cell Number ◽  
Culture Conditions ◽  
Shake Flask Culture ◽  
Amylase Production ◽  
Can Gio Mangrove

Amylases are one of the most important industrial enzymes and find applications in many areas such as textiles, chemicals, food, and pharmaceuticals. Most of the amylases are derived from microbes. The objective of the present study was to evaluate amylase production by a bacterium isolated from the Can Gio mangrove forest. The bacterium was identified as a species of genus Bacillus based on morphological and biochemical characteristics. The analysis of 16S rRNA sequences was then confirmed that this strain belonged to Bacillus amyloliquefaciens species (100% similarity). The effect of culture conditions such as temperature, pH, and carbon sources on amylase production through shake-flask culture was investigated. Maximum amylase activity of 904 IU/mL was obtained after 24 h of cultivation in LB medium containing 1% soluble starch at 35oC and pH 7.0. The highest enzyme activity of 1279 IU/mL was achieved in the bioreactor after 30 h of cultivation at optimum conditions. In addition, B. amyloliquefaciens M37 can grow on soybean meal medium. The high bacterial cell number of 456 × 109 CFU/g and amylase activity of 1039 IU/g were obtained after 36 h of cultivation. This newly isolated B. amyloliquefaciens M37 could be a potential producer for industrial amylase production and probiotics with commercial implications.

l-THYROXINE, CORTISOL AND DIET AFFECT THE LEVEL OF AMYLASE IN THE PAROTID GLAND OF DEVELOPING RATS

1980 ◽  
Vol 87 (1) ◽  
pp. 65-71 ◽  
Author(s):  
MASAYOSHI KUMEGAWA ◽  
NORIHIKO MAEDA ◽  
TOSHIHIKO YAJIMA ◽  
TAISHIN TAKUMA ◽  
EIKO IKEDA ◽  
...  
Keyword(s):  
Body Weight ◽  
Enzyme Activity ◽  
Parotid Gland ◽  
Amylase Activity ◽  
Synergistic Effects ◽  
Dietary Factors ◽  
Adult Rats ◽  
Early Increase ◽  
Adrenalectomized Rats ◽  
Intact Rats

The effects of cortisol (10 μg/g body weight) and l-thyroxine (T4; 0·2 μg/g body weight) on the activity of parotid gland amylase in young rats were investigated. Administration of cortisol or T4 for 5 consecutive days from day 5 after birth caused the precocious appearance of amylase, T4 having almost twice the effect of cortisol. Cortisol and T4 did not have synergistic effects. In thyroidectomized-adrenalectomized rats, T4 increased amylase activity but cortisol did not. The increase in enzyme activity after day 20 was much less in rats thyroidectomized on day 10 than in rats adrenalectomized on day 10. These results suggest that T4 has a direct effect on the early increase of amylase activity (days 15–25) and that the action of glucocorticoid requires the presence of endogenous thyroid hormones. The hormone-induced level of amylase in intact rats was less than that of normal adult rats. Forced weaning of intact rats resulted in a further increase in amylase activity, suggesting that further amylase accumulation (after day 25) may be due to dietary factors.

scholarly journals Proteins as targets for high dilutions of drugs: Interaction between ?-amylase and mercuric chloride.

2021 ◽  
Vol 17 (2) ◽  
pp. 24-25
Author(s):  
Nirmal Chandra Sukul ◽  
Tandra Sarkar ◽  
Atheni Konar ◽  
Anirban Sukul
Keyword(s):  
Mercuric Chloride ◽  
Binding Sites ◽  
Low Dose ◽  
Soluble Starch ◽  
Low Doses ◽  
Substrate Interaction ◽  
Enzyme Substrate ◽  
High Dilutions ◽  
High Doses ◽  
Mother Tincture

Background: High dilutions of drugs, used in homeopathy, are usually applied by oral route or foliar spray. These dilutions first come in contact with membrane or circulating proteins. Ultra low doses of mercuric chloride, called potencies, promote activity of diastase or ?-amylase in terms of breakdown of starch, a polysaccharide into a disaccharide maltose in a cell-free medium in test tubes. Merc cor or HgCl2 in high doses inhibits the enzyme activity. Aims: To see (i) whether the high and ultra low dose effects of HgCl2 involve different binding sites of the enzyme and (ii) to find an explanation for the low dose effect of HgCl2 in spite of absence of its original molecules. Methodology: Merc cor mother tincture (147 mM HgCl2) in distilled water was used undiluted in this experiment. Merc cor 200c and 1000c were prepared from the mother tincture (MT) by successive dilution with water 1:100 followed by succussion in 200 and 1000 steps, respectively, and finally preserved in 90% EtOH. These potencies and blank 90% ethanol, were diluted with deionized, distilled (DD) water 1:1000 to minimize ethanol content in test solutions. Each test solution or control was mixed with the enzyme 1:10 just before experiment. The control consisted of DD water. An isothermal calorimetry (ITC) instrument was used to measure the interaction between soluble starch and ?-amylase mixed with each potency (200c/1000c) of Merc cor, its mother tincture, ethanol and control. ITC is a thermodynamic technique which helps in measuring directly very small amount of heat evolved during chemical reaction. Soluble starch 90 µM was injected into 300 µl of 15µM ?-amylase at 2 µl / injection. Twenty injections, one every 2 min, were given. The enzyme substrate interaction in terms of heat released (exothermic) or absorbed (endothermic) were monitored by the ITC instrument. All ITC measurements were calculated and analyzed statistically by an in-built software Origin 7. Results and discussion: The data are presented in figures. While Merc cor MT shows endothermic reaction, all its potencies, ethanol and water control show exothermic reactions. There is wide variation in enthalpy (?H), entropy (?S), binding constant (K) and Gibbs free energy change (?G) among the treatments with Merc cor MT, potencies, ethanol and also control. The results indicate that Merc cor MT and its potencies act on different binding sites of the enzyme. The variation in thermodynamic parameters suggest difference in binding interaction between the drug solutions and the enzyme. This in turn influences the enzyme substrate interaction as reported in earlier studies. The potencies are virtually water modified by the starting substance HgCl2. Conclusion: The mother tincture and potencies of mercuric chloride produce different effects on the enzyme substrate interaction. Potencies show wide variation in ?H, ?S, K and ?G values. It appears from the results that the drugs used in homeopathy produce dual action on proteins. At high doses they act on a binding site(s) but at ultra low doses they act on a different binding site(s). Proteins in an organism may serve as targets for initiation of action of homeopathic potencies.

scholarly journals Optimization, Purification, and Starch Stain Wash Application of Two Newα-Amylases Extracted from Leaves and Stems ofPergularia tomentosa

2017 ◽  
Vol 2017 ◽  
pp. 1-9 ◽  
Author(s):  
Imen Lahmar ◽  
Hanen El Abed ◽  
Bassem Khemakhem ◽  
Hafedh Belghith ◽  
Ferjani Ben Abdallah ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Enzyme Activity ◽  
Specific Activity ◽  
Amylase Activity ◽  
Detergent Industry ◽  
Sepharose Column ◽  
Stems And Leaves ◽  
Commercial Detergents ◽  
Starch Substrate

A continuous research is attempted to fulfil the highest industrial demands of natural amylases presenting special properties. Newα-amylases extracted from stems and leaves ofPergularia tomentosa, which is widespread and growing spontaneously in Tunisia, were studied by the means of their activities optimization and purification. Some similarities were recorded for the two identified enzymes: (i) the highest amylase activity showed a promoted thermal stability at 50°C; (ii) the starch substrate at 1% enhanced the enzyme activity; (iii) the twoα-amylases seem to be calcium-independent; (iv) Zn2+, Cu2+, and Ag2+were considered as important inhibitors of the enzyme activity. Following the increased gradient of elution on Mono Q-Sepharose column, an increase in the specific activity of 11.82-fold and 10.92-fold was recorded, respectively, for leaves and stems with the presence of different peaks on the purification profiles.Pergulariaamylases activities were stable and compatible with the tested commercial detergents. The combination of plant amylase and detergent allowed us to enhance the wash performance with an increase of 35.24 and 42.56%, respectively, for stems and leaves amylases. Characterized amylases were reported to have a promoted potential for their implication notably in detergent industry as well as biotechnological sector.

A New Saccharogenic Micromethod for Measurement of Amylase Activity in Biological Fluids

1970 ◽  
Vol 16 (4) ◽  
pp. 300-304 ◽  
Author(s):  
Klaus Lorentz ◽  
Detlef Oltmanns
Keyword(s):  
Standard Deviation ◽  
Blood Donors ◽  
Serum Amylase ◽  
Amylase Activity ◽  
Biological Fluids ◽  
Soluble Starch ◽  
Starch Digestion ◽  
Triphenyltetrazolium Chloride ◽  
Serum Amylase Activity ◽  
Apparently Healthy

Abstract To determine serum amylase activity we have quantitatively measured the glucose and maltose hydrolyzed from soluble starch by colorimetrically measuring the reduction of colorless triphenyltetrazolium chloride to a red formazan, which is dissolved in methanol. The method is suitable for use with microsamples of all biological fluids, and is specific for the final products of starch digestion. Values found for sera from 55 apparently healthy blood donors ranged from 0.15 to 1.55 (mean, 0.83; standard deviation, ±0.4) mg of glucose per ml per h, corresponding to 7.5 to 78 Somogyi units.

Isolation and production of thermostable α-amylase from thermophilic Anoxybacillus sp. KP1 from Diyadin hot spring in Ağri, Turkey

Biologia ◽  
2014 ◽  
Vol 69 (4) ◽  
Author(s):  
Fatma Matpan Bekler ◽  
Kemal Güven
Keyword(s):  
Enzyme Activity ◽  
Hot Spring ◽  
Inorganic Nitrogen ◽  
Sodium Dodecyl ◽  
Maximum Growth ◽  
Casamino Acid ◽  
Rrna Gene ◽  
Amylolytic Enzyme ◽  
Amylase Production ◽  
Physiological Tests

AbstractA novel amylolytic enzyme producing thermophilic bacterial strain KP1 from the Diyadin hot spring water in Ağri, Turkey, was isolated in the present study. Phylogenetic analysis based on the partial 16S rRNA gene, biochemical and physiological tests revealed that the strain KP1 belongs to the genus Anoxybacillus. The pH and temperature optima for the α-amylase production by Anoxybacillus sp. KP1 were 8.0 and 50°C, respectively, where the maximum growth was obtained at the 28th hour of incubation and the highest α-amylase activity was obtained at the 40th hour of incubation (8979.6 U/mL). The optimum pH and temperature for the enzyme activity were 8.0 and 60°C, respectively. The maximum α-amylase production was secreted in the presence of 2% (w/v) soluble starch (10837.7 U/mL). Among the various organic and inorganic nitrogen sources tested, while keeping the beef extract concentration constant, casamino acid (14310.6 U/mL), urea (14126 U/mL), and tryptone (13217.2 U/mL) at a concentration of 2% gave the maximum α-amylase production. The enzyme activity was enhanced in the presence of 1.5 mM Mn2+ (123%), whereas it was strongly inhibited 1.5 mM by Hg2+. Inhibition by 89% was obtained also with sodium dodecyl sulphate (1%). The enzyme was found to be relatively stable at a range of pH and temperature.

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