Comparative analysis of thermostability of extracellular inulinase activity from Aspergillus fumigatus with commercially available (Novozyme) inulinase [An article from: Bioresource Technology]
Book Details
Author(s)P.K. Gill, R.K. Manhas, P. Singh
PublisherElsevier
ISBN / ASINB000RR5TOI
ISBN-13978B000RR5TO7
AvailabilityAvailable for download now
Sales Rank99,999,999
MarketplaceUnited States 🇺🇸
Description
This digital document is a journal article from Bioresource Technology, published by Elsevier in . The article is delivered in HTML format and is available in your Amazon.com Media Library immediately after purchase. You can view it with any web browser.
Description:
Thermostable inulinase activity was identified in the extracellular extract of Aspergillus fumigatus. At its optimum temperature of 60^oC, the ammonium sulphate fraction retained approximately 70% of its maximum activity after 72h incubation in the absence of inulin. The two isoforms of A. fumigatus inulinase were purified and their thermostability was studied. In the presence of inulin, isoform II was more thermostable when compared to other two fractions and retained approximately 54% activity after 3h at 60^oC. The higher thermostability of inulinase of A. fumigatus makes it a potential candidate for commercial production of fructose.
Description:
Thermostable inulinase activity was identified in the extracellular extract of Aspergillus fumigatus. At its optimum temperature of 60^oC, the ammonium sulphate fraction retained approximately 70% of its maximum activity after 72h incubation in the absence of inulin. The two isoforms of A. fumigatus inulinase were purified and their thermostability was studied. In the presence of inulin, isoform II was more thermostable when compared to other two fractions and retained approximately 54% activity after 3h at 60^oC. The higher thermostability of inulinase of A. fumigatus makes it a potential candidate for commercial production of fructose.
