Title of article :
Evidence of Tryptophan at or near Active Site of Glucoamylase I of Arthrobotrys amerospora
Author/Authors :
Norouzian, Dariush Pilot Biotechnology Dept. - Pasteur Institute of Iran , Akbarzadeh, Azim Pilot Biotechnology Dept. - Pasteur Institute of Iran , Rostami, Khosrow Biotechnology Center - IROST - Tehran , Nouri Inanlou, Davoud Pilot Biotechnology Dept. - Pasteur Institute of Iran , Farahmand, Behrokh Pilot Biotechnology Dept. - Pasteur Institute of Iran
Abstract :
Arthrobotrys amerospora (ATCC 34468) produced glucoamylase in a semi-synthetic medium containing
starch as a sole carbon source. Polyacrylamide gel electrophoresis of crude glucoamylase showed three
isoenzymes. They were designated as glu I, glu II and glu III according to their electrophoretic mobility.
These iso-glucoamylases were purified by column chromatography using DEAE-Sephadex A-50. The
major fraction, namely glu I, was subjected to various group specific reagents like NEM, idoacetamide,
PALP, DEP, Rose Bengal, NBS and acarbose. N-bromosuccinimide and acarbose totally inhibited glu I.
Hg2+
ion did not inhibit glu I activity at 25 m mol concentration. Glu I also showed raw starch activity.
Keywords :
Glucoamylase I , Tryptophan , Arthrobotrysamerospora
Journal title :
Astroparticle Physics
