Characterization of a Hydrophobic Amylase Inhibitor from Corn (Zea mays) Seeds with Activity Against Amylase from Fusarium verticillioides
نویسندگان
چکیده
منابع مشابه
Characterization of an a-Amylase with Broad Temperature Activity from an Acid-Neutralizing Bacillus cereus Strain
Bacillus sp. GUF8, isolated from acidic soil samples of a tea farm was identified as Bacillus cereus, based on 16S rDNA sequencing and standard bacterial identification methods. Following optimization of enzyme production, the resulting α-amylase was purified by acetone precipitation and ion exchange chromatography. Consequently, thermostability and kinetic parameters of the purified enzyme wer...
متن کاملA novel alpha-amylase inhibitor from amaranth (Amaranthus hypocondriacus) seeds.
The major alpha-amylase inhibitor (AAI) present in the seeds of Amaranthus hypocondriacus, a variety of the Mexican crop plant amaranth, is a 32-residue-long polypeptide with three disulfide bridges. Purified AAI strongly inhibits the alpha-amylase activity of insect larvae (Tribolium castaneum and Prostephanus truncatus) and does not inhibit proteases and mammalian alpha-amylases. AAI was sequ...
متن کاملCharacterization of the Α-amylase Inhibitor from the Seeds of Macrotyloma Uniflorum and Vigna Unguiculata
α-amylase inhibitors were purified and characterized from the seeds of Macrotyloma uniflorum (MUAI) and Vigna unguiculata (VUAI). MUAI was purified using CM-cellulose column while VUAI was purified using Poros HS-50 column followed by gel filtration on Sephadex G-75 column. The molecular weights of MUAI and VUAI as determined by gel filtration were 26.91 kD and 21.89 kD respectively. Both MUAI ...
متن کاملPurification and characterization of a-amylase from rat pancreatfic acinar carcinoma Comparison with pancreatic a-amylase
a-Amylase was purified to apparent homogeneity from normal pancreas and a transplantable pancreatic acinar carcinoma of the rat by affinity chromatography on a-glucohydrolase inhibitor (a-GHI) bound to aminohexyl-Sepharose 4B. Recovery was 95-100% for both pancreas and tumour a-amylases. They were monomeric proteins, with Mr approx. 54000 on SDS/polyacrylamide-gel electrophoresis. Isoelectric f...
متن کاملcharacterization of an a-amylase with broad temperature activity from an acid-neutralizing bacillus cereus strain
bacillus sp. guf8, isolated from acidic soil samples of a tea farm was identified as bacillus cereus, based on 16s rdna sequencing and standard bacterial identification methods. following optimization of enzyme production, the resulting α-amylase was purified by acetone precipitation and ion exchange chromatography. consequently, thermostability and kinetic parameters of the purified enzyme wer...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Phytopathology®
سال: 2003
ISSN: 0031-949X,1943-7684
DOI: 10.1094/phyto.2003.93.8.917