scholarly journals Production of amylases by Aspergillus tamarii

1999 ◽  
Vol 30 (2) ◽  
pp. 157-162 ◽  
Author(s):  
Fabiana Guillen Moreira ◽  
Francieli Arrias de Lima ◽  
Sophia Renata Fazzano Pedrinho ◽  
Veridiana Lenartovicz ◽  
Cristina Giatti Marques de Souza ◽  
...  
Keyword(s):  
Carbon Source ◽  
Ion Exchange ◽  
Filamentous Fungus ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Aspergillus Tamarii ◽  
Ph Values ◽  
Wide Range ◽  
Initial Culture ◽  
Static Cultivation

A strain of Aspergillus tamarii, a filamentous fungus isolated from soil, was able to produce both <FONT FACE="Symbol">a</FONT>-amylase and glucoamylase activities in mineral media supplemented with 1% (w/v) starch or maltose as the carbon source. Static cultivation led to significantly higher yields than those obtained using shaking culture. The production of amylases was tolerant to a wide range of initial culture pH values (from 4 to 10) and temperature (from 25 to 42oC). Two amylases, one <FONT FACE="Symbol">a</FONT>-amylase and one glucoamylase, were separated by ion exchange chromatography. Both partially purified enzymes had optimal activities at pH values between 4.5 and 6.0 and were stable under acid conditions (pH 4.0-7.0). The enzymes exhibited optimal activities at temperatures between 50o and 60o C and were stable for more than ten hours at 55oC.

scholarly journals Submerged fermentation of amylase enzyme by Aspergillus flavus using Cocos nucifera meal

1970 ◽  
Vol 6 (2) ◽  
pp. 75-87 ◽  
Author(s):  
M Arunsasi ◽  
S Manthiri Kani ◽  
G Jegadeesh ◽  
M Ravikumar
Keyword(s):  
Heavy Metals ◽  
Carbon Source ◽  
Ion Exchange ◽  
Aspergillus Flavus ◽  
Cocos Nucifera ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Soil Samples ◽  
Physico Chemical ◽  
Sds Page

Soil samples were collected from the coastal region of Neendakara, along the West cost of Kerala, India. 15 fungal species were isolated and identified by using lacto phenol cotton blue staining method. From this, Aspergillus flavus was tested in Starch Hydrolysis Agar Medium for its amylase enzyme production under sumerged aerobic fermentation with different physico- chemical properties of substrates. Cocos nucifera meal was used as a carbon source. Heavy metals were added to these medium and were used as a modified medium. The effect of different carbon source, nitrogen compound and physico-chemical conditions like temperature, pH and incubation periods were studied for derivation of amylase enzyme. The molecular weight of enzyme was determined by SDS –PAGE. The role of heavy metals was determined by ion exchange chromatography. Cocos nucifera meal medium with dextrose has shown the highest amylase production at pH 6.0 and temperature of 30ºC with protein content of 201μg/ml; 98.4μg/ml and dry biomass of 1.28μg/ml. Keywords: Soil samples; A. flavus; amylase; SDS-PAGE; Ion exchange chromatography; submerged aerobic fermentation DOI: 10.3126/kuset.v6i2.4015Kathmandu University Journal of Science, Engineering and Technology Vol.6. No II, November, 2010, pp.75-87

Studies on an Inhibitor of Plasminogen Activation in Human Serum

1973 ◽  
Vol 30 (02) ◽  
pp. 414-424 ◽  
Author(s):  
Ulla Hedner
Keyword(s):  
Ion Exchange ◽  
Human Serum ◽  
Antithrombin Iii ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Specific Adsorption ◽  
Partial Purification ◽  
Plasminogen Activation ◽  
Preparative Electrophoresis

SummaryA procedure is described for partial purification of an inhibitor of the activation of plasminogen by urokinase and streptokinase. The method involves specific adsorption of contammants, ion-exchange chromatography on DEAE-Sephadex, gel filtration on Sephadex G-200 and preparative electrophoresis. The inhibitor fraction contained no antiplasmin, no plasminogen, no α1-antitrypsin, no antithrombin-III and was shown not to be α2 M or inter-α-inhibitor. It contained traces of prothrombin and cerulo-plasmin. An antiserum against the inhibitor fraction capable of neutralising the inhibitor in serum was raised in rabbits.

Review on the Application of Mixed-mode Chromatography for Separation of Structure Isoforms

2018 ◽  
Vol 20 (1) ◽  
pp. 56-60 ◽  
Author(s):  
Tsutomu Arakawa
Keyword(s):  
Ion Exchange ◽  
Mixed Mode ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Charged State ◽  
Partial Structure ◽  
Reverse Phase ◽  
Oligomer Formation ◽  
Structure Rearrangement ◽  
Disulfide Scrambling

Proteins often generate structure isoforms naturally or artificially due to, for example, different glycosylation, disulfide scrambling, partial structure rearrangement, oligomer formation or chemical modification. The isoform formations are normally accompanied by alterations in charged state or hydrophobicity. Thus, isoforms can be fractionated by reverse-phase, hydrophobic interaction or ion exchange chromatography. We have applied mixed-mode chromatography for fractionation of isoforms for several model proteins and observed that cation exchange Capto MMC and anion exchange Capto adhere columns are effective in separating conformational isoforms and self-associated oligomers.

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