Production of amylase by soil fungi and partial biochemical characterization of amylase of a selected strain (Aspergillus fumigatus Fresenius)

1993 ◽  
Vol 39 (7) ◽  
pp. 681-685 ◽  
Author(s):  
Claudia M. Domingues ◽  
Rosane M. Peralta

Filamentous fungi from soil were screened for their ability to produce amylases in semisolid and liquid media with wheat bran. A selected strain identified as Aspergillus fumigatus Fresenius showed high enzymatic activity for α-amylase and glucoamylase. The maximal yield of these amylases was obtained when lignocellulosic materials were the carbon sources. The optimal pH and temperature were 6.0 and 50 °C, respectively, for both enzymes. α-Amylase activity was more thermostable than glucoamylase activity.Key words: amylolitic fungi, α-amylase, glucoamylase, Aspergillus fumigatus.

Author(s):  
Mirco Dindo ◽  
Egidia Costanzi ◽  
Marco Pieroni ◽  
Claudio Costantini ◽  
Giannamaria Annunziato ◽  
...  

ChemBioChem ◽  
2011 ◽  
Vol 12 (5) ◽  
pp. 711-714 ◽  
Author(s):  
Naoki Kato ◽  
Hirokazu Suzuki ◽  
Hiroshi Takagi ◽  
Masakazu Uramoto ◽  
Shunji Takahashi ◽  
...  

2014 ◽  
Vol 2014 ◽  
pp. 1-11 ◽  
Author(s):  
Hana Maalej ◽  
Hanen Ben Ayed ◽  
Olfa Ghorbel-Bellaaj ◽  
Moncef Nasri ◽  
Noomen Hmidet

Amylase production and biochemical characterization of the crude enzyme preparation fromPseudomonas stutzeriAS22 were evaluated. The highestα-amylase production was achieved after 24 hours of incubation in a culture medium containing 10 g/L potato starch and 5 g/L yeast extract, with initial pH 8.0 at 30°C under continuous agitation at 200 rpm. The optimum temperature and pH for the crudeα-amylase activity were 60°C and 8.0, respectively. The effect of different salts was evaluated and it was found that bothα-amylase production and activity were Ca2+-dependent. The amylolytic preparation was found to catalyze exceptionally the formation of very high levels of maltotetraose from starch (98%, w/w) in the complete absence of glucose since the initial stages of starch hydrolysis (15 min) and hence would have a potential application in the manufacturing of maltotetraose syrups.


2000 ◽  
Vol 275 (2) ◽  
pp. 279-285 ◽  
Author(s):  
Abul H.J. Ullah ◽  
Kandan Sethumadhavan ◽  
X.G. Lei ◽  
Edward J. Mullaney

2021 ◽  
Vol 18 ◽  
Author(s):  
Yan Shan ◽  
Junjie Shang ◽  
Dongfang Zhang ◽  
Yinshan Cui ◽  
Yi Wang ◽  
...  

Background: Amylase used in the market is mostly medium-temperature enzyme or high-temperature enzyme and has poor enzyme activity under low-temperature environment. Acid α-amylase can be used to develop digestion additives in the pharmaceutical and healthcare industries. The amino acid sequence and structural differences among α-amylases obtained from various organisms are high enough to confer interesting biochemical diversity to the enzymes. However, low- temperature (0-50℃) amylase, with an optimum temperature and heat sensitivity, has a greater potential value than medium (50-80℃) and high (80-110℃) temperature amylases. Methodology: The gene amy48 from encoding extracellular α-amylase in Bacillus subtilis YX48 was successfully cloned into the pET30a (+) vector and expressed in Escherichia coli BL21 (DE3) for biochemical characterization. Results and Conclusion: The molecular weight of α-amylase was 75 kDa. The activity of α-amylase was not affected by Ca2+, and Amy48 had the best activity at pH 5.0 and 37℃. AMY48 has high stability over a narrow pH and temperature range (5.0-8.0 and 30-45℃). Amylase activity was strongly inhibited by Zn2+, Mn2+, Cu2+, and Fe2+ ions, but Na+, K+, and Co2+ ions stimulate its activity slightly. The purified enzyme showed gradually reduced activity in the presence of detergents. However, it was remarkably stable against EDTA and urea.


2013 ◽  
Vol 12 (6) ◽  
pp. 853-863 ◽  
Author(s):  
Karine Lambou ◽  
Andrea Pennati ◽  
Isabel Valsecchi ◽  
Rui Tada ◽  
Stephen Sherman ◽  
...  

ABSTRACTThe choline oxidase (CHOA) and betaine aldehyde dehydrogenase (BADH) genes identified inAspergillus fumigatusare present as a cluster specific for fungal genomes. Biochemical and molecular analyses of this cluster showed that it has very specific biochemical and functional features that make it unique and different from its plant and bacterial homologs.A. fumigatusChoAp catalyzed the oxidation of choline to glycine betaine with betaine aldehyde as an intermediate and reduced molecular oxygen to hydrogen peroxide using FAD as a cofactor.A. fumigatusBadhp oxidized betaine aldehyde to glycine betaine with reduction of NAD+to NADH. Analysis of theAfchoAΔ::HPHandAfbadAΔ::HPHsingle mutants and theAfchoAΔAfbadAΔ::HPHdouble mutant showed thatAfChoAp is essential for the use of choline as the sole nitrogen, carbon, or carbon and nitrogen source during the germination process.AfChoAp andAfBadAp were localized in the cytosol of germinating conidia and mycelia but were absent from resting conidia. Characterization of the mutant phenotypes showed that glycine betaine inA. fumigatusfunctions exclusively as a metabolic intermediate in the catabolism of choline and not as a stress protectant. This study inA. fumigatusis the first molecular, cellular, and biochemical characterization of the glycine betaine biosynthetic pathway in the fungal kingdom.


2021 ◽  
Vol 9 (8) ◽  
pp. 1655
Author(s):  
Marcus Stabel ◽  
Tabea Schweitzer ◽  
Karoline Haack ◽  
Pascal Gorenflo ◽  
Habibu Aliyu ◽  
...  

Anaerobic fungi are prime candidates for the conversion of agricultural waste products to biofuels. Despite the increasing interest in these organisms, their growth requirements and metabolism remain largely unknown. The isolation of five strains of anaerobic fungi and their identification as Neocallimastix cameroonii, Caecomyces spec., Orpinomyces joyonii, Pecoramyces ruminantium, and Khoyollomyces ramosus, is described. The phylogeny supports the reassignment of Neocallimastix californiae and Neocallimastix lanati to Neocallimastix cameroonii and points towards the redesignation of Cyllamyces as a species of Caecomyces. All isolated strains including strain A252, which was described previously as Aestipascuomyces dubliciliberans, were further grown on different carbon sources and the produced metabolites were analyzed; hydrogen, acetate, formate, lactate, and succinate were the main products. Orpinomyces joyonii was lacking succinate production and Khoyollomyces ramosus was not able to produce lactate under the studied conditions. The results further suggested a sequential production of metabolites with a preference for hydrogen, acetate, and formate. By comparing fungal growth on monosaccharides or on the straw, a higher hydrogen production was noticed on the latter. Possible reactions to elevated sugar concentrations by anaerobic fungi are discussed.


2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Natalie C. Bamford ◽  
François Le Mauff ◽  
Jaime C. Van Loon ◽  
Hanna Ostapska ◽  
Brendan D. Snarr ◽  
...  

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