Starch Blocking Stability of the Phaseolus vulgaris Alpha-Amylase Inhibitor (α-AI1)

2008 ◽  
Vol 4 (1) ◽  
pp. 9-19 ◽  
Author(s):  
Wokadala C. Obiro ◽  
Tao Zhang ◽  
Bo Jiang
Keyword(s):  
Phaseolus Vulgaris ◽  
Alpha Amylase ◽  
Amylase Inhibitor ◽  
Alpha Amylase Inhibitor

scholarly journals Thermal Stability and Digestibility of .ALPHA.-Amylase Inhibitor from Phaseolus vulgaris cultivar Tora.

2000 ◽  
Vol 47 (2) ◽  
pp. 158-162 ◽  
Author(s):  
Hideki YOSHIKAWA ◽  
Makoto KOTARU ◽  
Chie TANAKA ◽  
Tsuneo IKEUCHI ◽  
Makoto KAWABATA
Keyword(s):  
Thermal Stability ◽  
Phaseolus Vulgaris ◽  
Alpha Amylase ◽  
Amylase Inhibitor ◽  
Alpha Amylase Inhibitor

scholarly journals Evaluation of Inhibitory Activity, Purification and X-Ray Crystallography of Alpha—Amylase Inhibitor from Phaseolus Vulgaris Cultivars of Uttarakhand

2021 ◽  
Author(s):  
Ravinder Singh ◽  
Anoop Kumar Dobriyal ◽  
Rattan Deep Singh ◽  
Patricio De los Rios-Escalante
Keyword(s):  
Phaseolus Vulgaris ◽  
Crude Extract ◽  
Inhibitory Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Heat Stability ◽  
Alpha Amylase ◽  
Native Page ◽  
X Ray Crystallography ◽  
Amylase Inhibitor ◽  
Alpha Amylase Inhibitor

Abstract The present work is based on analysis of inhibitory activity of alpha-amylase inhibitor in selected cultivars of Phaseolus vulgaris of Uttarakhand. Fifteen samples were assessed for inhibitory activity of alpha-amylase inhibitor. Significant variations were found in different cultivars. Crude extract of alpha-amylase inhibitor from sample PUR (Purola) have shown maximum inhibitory activity (70.2 ± 0.84). Crude extract of all the cultivars have shown considerable variations in inhibitory activity in the temperature ranging from 20ºC to 100ºC. Based on inhibitory activity and heat stability profile, the alpha amylase inhibitor was purified from PUR cultivar. The purified inhibitor was found to be stable even at 90ºC with an inhibitory activity of 97.20 ±0.09. The molecular weight of purified inhibitor on Native PAGE (Polyacrylamide gel electrophoresis) was found to be 31kd, consisting of two subunits of 17kd and 14kd on SDS-PAGE.

scholarly journals Purification and some properties of an .ALPHA.-amylase inhibitor from cranberry bean (Phaseolus vulgaris)

1987 ◽  
Vol 51 (2) ◽  
pp. 577-578 ◽  
Author(s):  
Makoto KOTARU ◽  
Koichi SAITO ◽  
Hideki YOSHIKAWA ◽  
Tsuneo IKEUCHI ◽  
Fumio IBUKI
Keyword(s):  
Phaseolus Vulgaris ◽  
Alpha Amylase ◽  
Amylase Inhibitor ◽  
Alpha Amylase Inhibitor
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