Purification and characterization of an invertase from Candida utilis: comparison with natural and recombinant yeast invertases

Journal of Biotechnology
F P ChávezJ A Cremata

Abstract

A periplasmic invertase from the yeast Candida utilis was purified to homogeneity from cells fully derepressed for invertase synthesis. The enzyme was purified by successive Sephacryl S-300, and affinity chromatography and shown to be a dimeric glycoprotein composed of two identical monomer subunits with an apparent molecular mass of 150 kDa. After EndoH treatment, the deglycosylated protein showed an apparent molecular weight of 60 kDa. The apparent K(m) values for sucrose and raffinose were 11 and 150 mM, respectively, similar to those reported in Saccharomyces cerevisiae. The range of optimum temperature was 60-75 degrees C. The optimum pH was 5.5 and the enzyme was stable over pH range 3-6.

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Citations

Feb 5, 2014·Journal of Food Science and Technology·Younes GhasemiSara Rasoul-Amini
Jun 18, 2011·Microbiology·Christoph BuerthDenis Tielker
Apr 17, 2016·New Biotechnology·Sebastian C Spohner, Peter Czermak
May 18, 2016·Biochemistry Research International·Arpita Singh, Debjani Mandal
Jun 9, 2018·Critical Reviews in Food Science and Nutrition·Bilal Muhammad KhanYang Liu
Aug 15, 2015·Biotechnology and Applied Biochemistry·Grecia De León-GonzálezMarco Rito-Palomares
Feb 18, 2021·Journal of Food Biochemistry·Letícia Mara RasboldAlexandre Maller
Oct 24, 2006·Journal of Biotechnology·Iraj GhaziFrancisco J Plou
Jun 22, 2006·Journal of Agricultural and Food Chemistry·Haq Nawaz BhattiMunir A Sheikh

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