Literature DB >> 3132328

Properties of the raw-starch digesting amylase of Aspergillus sp. K-27: a synergistic action of glucoamylase and alpha-amylase.

J I Abe1, K Nakajima, H Nagano, S Hizukuri, K Obata.   

Abstract

Glucoamylase and alpha-amylase have been purified from a crude enzyme preparation of Aspergillus sp. K-27. The former was thermostable and seemed to have a "starch-binding site", judging from the results of a kinetic study, and the latter synergistically enhanced the degradation of starch granules with glucoamylase.

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Year:  1988        PMID： 3132328     DOI： 10.1016/0008-6215(88)80158-7

Source DB:  PubMed          Journal:  Carbohydr Res        ISSN： 0008-6215            Impact factor:   2.104


  4 in total

Review 1.  Thermophilic fungi: their physiology and enzymes.

Authors:  R Maheshwari; G Bharadwaj; M K Bhat
Journal:  Microbiol Mol Biol Rev       Date:  2000-09       Impact factor: 11.056

2.  Purification and characterization of periplasmic alpha-amylase from Xanthomonas campestris K-11151.

Authors:  J Abe; N Onitsuka; T Nakano; Y Shibata; S Hizukuri; E Entani
Journal:  J Bacteriol       Date:  1994-06       Impact factor: 3.490

3.  Characterization of thermostable cyclodextrinase from Clostridium thermohydrosulfuricum 39E.

Authors:  B C Saha; J G Zeikus
Journal:  Appl Environ Microbiol       Date:  1990-09       Impact factor: 4.792

4.  Cloning of a novel thermostable glucoamylase from thermophilic fungus Rhizomucor pusillus and high-level co-expression with α-amylase in Pichia pastoris.

Authors:  Zhenggui He; Lujia Zhang; Youzhi Mao; Jingchao Gu; Qi Pan; Sixing Zhou; Bei Gao; Dongzhi Wei
Journal:  BMC Biotechnol       Date:  2014-12-24       Impact factor: 2.563
  4 in total

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