scholarly journals Purification and action pattern on soluble starch of .ALPHA.-amylase from sugar cane leaves.

1990 ◽  
Vol 54 (3) ◽  
pp. 849-850 ◽  
Author(s):  
Masaru MIYAGI ◽  
Hirosuke OKU ◽  
Isao CHINEN
Keyword(s):  
Sugar Cane ◽  
Soluble Starch ◽  
Alpha Amylase ◽  
Action Pattern

Purification and Action Pattern on Soluble Starch ofα-Amylase from Sugar Cane Leaves

1990 ◽  
Vol 54 (3) ◽  
pp. 849-850
Author(s):  
Masaru Miyagi ◽  
Hirosuke Oku ◽  
Isao Chinen
Keyword(s):  
Sugar Cane ◽  
Soluble Starch ◽  
Action Pattern

scholarly journals Biochemical and Structural Characterization of Amy1: An Alpha-Amylase from Cryptococcus flavus Expressed in Saccharomyces cerevisiae

2011 ◽  
Vol 2011 ◽  
pp. 1-7 ◽  
Author(s):  
Alexsandro Sobreira Galdino ◽  
Roberto Nascimento Silva ◽  
Muriele Taborda Lottermann ◽  
Alice Cunha Morales Álvares ◽  
Lídia Maria Pepe de Moraes ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Soluble Starch ◽  
Alpha Amylase ◽  
Enzyme Specificity ◽  
Wild Type ◽  
Spectra Analysis ◽  
Exclusion Chromatography ◽  
The Difference ◽  
Thermal Stability Of

An extracellular alpha-amylase (Amy1) whose gene from Cryptococcus flavus was previously expressed in Saccharomyces cerevisiae was purified to homogeneity (67 kDa) by ion-exchange and molecular exclusion chromatography. The enzyme was activated by NH4+ and inhibited by Cu+2 and Hg+2. Significant biochemical and structural discrepancies between wild-type and recombinant α-amylase with respect to Km values, enzyme specificity, and secondary structure content were found. Far-UV CD spectra analysis at pH 7.0 revealed the high thermal stability of both proteins and the difference in folding pattern of Amy1 compared with wild-type amylase from C. flavus, which reflected in decrease (10-fold) of enzymatic activity of recombinant protein. Despite the differences, the highest activity of Amy1 towards soluble starch, amylopectin, and amylase, in contrast with the lowest activity of Amy1w, points to this protein as being of paramount biotechnological importance with many applications ranging from food industry to the production of biofuels.

scholarly journals Biochemical characterisation of α-amylase in two aphid species, Aphis fabae Scopoli (Hemiptera: Aphididae) and A. gossypii Glover (Hemiptera: Aphididae)

2014 ◽  
Vol 50 (No. 2) ◽  
pp. 84-89 ◽  
Author(s):  
A. Darvishzadeh ◽  
A. Bandani ◽  
S.Q. Mousavi
Keyword(s):  
Soluble Starch ◽  
Aphid Species ◽  
Aphis Fabae ◽  
Alpha Amylase ◽  
Insect Species ◽  
Zymogram Analysis ◽  
Biochemical Characterisation ◽  
Optimum Ph ◽  
Optimum Ph And Temperature ◽  
Alpha Amylases

We identify and characterise α-amylases of the two aphid species, A. fabae and A. gossypi. To do this, α-amylases of the two insect species were extracted and their activities were determined using 1% soluble starch. Results showed that α-amylase, which hydrolyses starch, is present in both aphids. Also, it was shown that optimum pH and temperature for the α-amylases of both species is 7.0 and 40°C, respectively. Gel assays using zymogram analysis showed that in both aphid species more than one isoform (two isoforms) of α-amylases hydrolyszing carbohydrates are present.  

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