Literature DB >> 19508217

Invertase from hyper producer strain of Aspergillus niger: physiochemical properties, thermodynamics and active site residues heat of ionization.

Habibullah Nadeem1, Muhammad Hamid Rashid, Muhammad Riaz, Bibi Asma, Muhammad Rizwan Javed, Raheela Perveen.   

Abstract

Here we report for the first time heat of ionization of invertase (E.C.3.2.1.26) active site residues from hyper-producer strain of Aspergillus niger (34.1 U ml(-1)), along with its physiochemical properties, kinetics and thermodynamics of stability-function. The Invertase showed great potential for industry as being highly efficient (k(cat) = 24167 s(-1) at 65 degrees C, pH 5.0) and stable (half life= 12 h at 56 degrees C).

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Year:  2009        PMID: 19508217     DOI: 10.2174/092986609789055322

Source DB:  PubMed          Journal:  Protein Pept Lett        ISSN: 0929-8665            Impact factor:   1.890


  2 in total

1.  Purification and biochemical characterization of an extracellular β-d-fructofuranosidase from Aspergillus sp.

Authors:  Lynette Lincoln; Sunil S More
Journal:  3 Biotech       Date:  2018-01-20       Impact factor: 2.406

2.  Identification and Immobilization of an Invertase With High Specific Activity and Sucrose Tolerance Ability of Gongronella sp. w5 for High Fructose Syrup Preparation.

Authors:  Gang Zhou; Can Peng; Xiaosa Liu; Fei Chang; Yazhong Xiao; Juanjuan Liu; Zemin Fang
Journal:  Front Microbiol       Date:  2020-04-09       Impact factor: 5.640

  2 in total

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