Document Details

Document Type : Article In Journal 
Document Title :
Extraction and characterization of alpha-amylase inhibitor from some cereals and legumes
فصل ودراسة خواص مثبط إنزيم الألفا أميليز من بعض الحبوب والبقوليات
 
Document Language : English 
Abstract : ABSTRACT Alpha-amylase inhibitor extracted from different sources i.e. wheat grains (sohag 2 and Giza 164), legume seeds such as Cow pea (Carim 7 and Giza 3), and Kidney bean (Giza 6 and Giza 133) was purified and tested for activity using human salivary and pancreatic alpha-amylase. Results showed that the alpha-amylase inhibitor activity from samples studied were 120 to 285 unit / mg protein. The inhibitor was found to be stable at pH range from 2 to 4. It was also stable to digestion by proteolytic enzymes (pepsin and trypsin). The inhibition was faster at 37 oC than at 25 oC, The results showed that the degree of thermal stability of alpha-amylase inhibitor extracted from Kidney bean (Giza 133) was at 35-37 oC, activity was decreased on 50 oC for 5 hr. Increased of pre-incubation time between inhibitor and both alpha-amylase enzymes at 37 oC increased the rate of inhibition of these enzymes and the complex formation between them from 60 – 80 % in 30 min. while addition of these enzymes to the mixture containing inhibitor and substrate (without pre-incubation) decrease the percent inhibition. Therefore, an evidence of specific interference of the alpha-amylase inhibitor with starch availability was established. Such possibilities will have valuable interest in the field of special dietary food preparations for diabetes and over weight reduction purposes. Key Words: Alpha-amylase inhibitor; Wheat; Legumes. 
ISSN : 95 
Journal Name : Egypt. J. Food Sci. 
Volume : 35 
Issue Number : 2 
Publishing Year : 1428 AH
2007 AD 
Article Type : Article 
Added Date : Saturday, September 3, 2011 

Researchers

Researcher Name (Arabic)Researcher Name (English)Researcher TypeDr GradeEmail
محمد حسين مدكورMadkour, Mohamed HusseinResearcherDoctoratemadkour55@yahoo.com

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