Volume 3, Issue 3 And 4 (7-1999)                   ibj 1999, 3(3 And 4): 103-107 | Back to browse issues page

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Norouzian D, Akbarzadeh A, Rostami K, Nouri Inanlou D, Farahmand B. Evidence of Tryptophan at or near Active Site of Glucoamylase I of Arthrobotrys amerospora. ibj. 1999; 3 (3 and 4) :103-107
URL: http://ibj.pasteur.ac.ir/article-1-843-en.html
Arthrobotrysamerospora (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.
Type of Study: Full Length |

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