Literature DB >> 14768025

A thermostable maltose-tolerant alpha-amylase from Aspergillus tamarii.

Fabiana Guillen Moreira1, Veridiana Lenartovicz, Rosane Marina Peralta.   

Abstract

An homogeneous fraction of alpha-amylase from Aspergillus tamarii was obtained by means of a very easy purification procedure. The enzyme is a glycoprotein containing 32% saccharide and MW of 37.5 kDa. Optimal of pH and temperature with starch as substrate were 4.5-6.5 and 50-55 degrees C. The enzyme was stable for several hours at temperature up to 65 degrees C. Starch, amylose, and amylopectin were the substrates preferentially hydrolysed and maltose and maltotriose were the main end products. The values of K(M) and V(max) for starch were 2 g/l and 880 micromoles reducing sugars/min.mg of protein, respectively. The purified enzyme was remarkably insensitive to end product inhibition, being only slightly inhibited by maltose and glucose up to 1.0 M.

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Year:  2004        PMID: 14768025     DOI: 10.1002/jobm.200310302

Source DB:  PubMed          Journal:  J Basic Microbiol        ISSN: 0233-111X            Impact factor:   2.281


  9 in total

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Journal:  J Clin Microbiol       Date:  2007-08-15       Impact factor: 5.948

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9.  Purification and characterization of α-amylase from Trichoderma pseudokoningii.

Authors:  Wesam H Abdulaal
Journal:  BMC Biochem       Date:  2018-06-14       Impact factor: 4.059

  9 in total

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