Production and properties of a bacterial thermostable exo-inulinase.

نویسندگان

  • K Uzunova
  • A Vassileva
  • M Kambourova
  • V Ivanova
  • D Spasova
  • R Mandeva
  • A Derekova
  • A Tonkova
چکیده

Inulinase and Invertase Activities, Thermophilic Bacilli, Enzyme Thermostability Enzyme production of newly isolated thermophilic inulin-degrading Bacillus sp. 11 strain was studied by batch cultivation in a fermentor. The achieved inulinase and invertase activities after a short growth time (4.25 h) were similar or higher compared to those reported for other mesophilic aerobic or anaerobic thermophilic bacterial producers and yeasts. The investigated enzyme belonged to the exo-type inulinases and splitted-off inulin, sucrose and raffinose. It could be used at temperatures above 65 degrees C and pH range 5.5-7.5. The obtained crude enzyme preparation possessed high thermostability. The residual inulinase and invertase activities were 92-98% after pretreatment at 65 degrees C for 60 min in the presence of substrate inulin.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Production of Inulinase by Fusarium sp. and its Application for Fructooligosaccharide Production for use as Prebiotics

Fructooligosaccharides (FOS) are useful due to their applications in food and pharmaceutical industry. Fusarium spp., isolated from dahlia rhizosphere, produced endoinulinases in a medium containing inulin or sucrose as carbon substrate. Characterisation of exo-inulinase and production of FOS were investigated. Temperature and pH optimum of the enzyme was found to be 60 °C and pH 6.0, respectiv...

متن کامل

Comparative study of two purified inulinases from thermophile Thielavia Terrestris NRRL 8126 and mesophile Aspergillus Foetidus NRRL 337 grown on Cichorium Intybus l

Thirty fungal species grown on Cichorium intybus L. root extract as a sole carbon source, were screened for the production of exo-inulinase activities. The thermophile Thielavia terrestris NRRL 8126 and mesophile Aspergillus foetidus NRRL 337 gave the highest production levels of inulinases I & II at 50 and 24 ºC respectively. Yeast extract and peptone were the best nitrogen sources for highest...

متن کامل

Exo-inulinase of Aspergillus niger N402: A hydrolytic enzyme with significant transfructosylating activity

The purified exo-inulinase enzyme ofAspergillus nigerN402 (AngInuE; heterologously expressed in Escherichia coli) displayed a sucrose:inulin (S/I) hydrolysis ratio of 2.3, characteristic for a typical exo-inulinase. The enzyme also had significant transfructosylating activity with increasing sucrose concentrations, producing various oligosaccharides. The AngInuE protein molecular mass was 57 kD...

متن کامل

Production of Inulinases: Recent Advances

Inulinases constitute an important class of enzymes for production of fructose and fructooligosaccharides, which are extensively used in pharmaceutical and food industry. The production of inulinases has been reported from various fungal, yeast and bacterial strains. The inulinases characterized until now show considerable variability with respect to biophysical and biochemical characteristics....

متن کامل

Purification, characterization, gene cloning and preliminary X-ray data of the exo-inulinase from Aspergillus awamori.

Extracellular exo-inulinase has been isolated from a solid-phase culture of the filamentous fungus Aspergillus awamori var. 2250. The apparent molecular mass of the monomer enzyme was 69 +/- kDa, with a pI of 4.4 and a pH optimum of 4.5. The enzyme hydrolysed the beta-(2-->1)-fructan (inulin) and beta-(2-->6)-fructan (levan) via exo-cleavage, releasing fructose. The values for the Michaelis con...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Zeitschrift fur Naturforschung. C, Journal of biosciences

دوره 56 11-12  شماره 

صفحات  -

تاریخ انتشار 2001