Home
Resources
Publications
Purification and Characterization of an Invertase From Candida Utilis: Comparison With Natural and Recombinant Yeast Invertases

Purification and Characterization of an Invertase From Candida Utilis: Comparison With Natural and Recombinant Yeast Invertases

F P Chávez, L Rodriguez, J Díaz, J M Delgado, J A Cremata

J Biotechnol. 1997 Feb 28;53(1):67-74.

PMID: 9165761

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP9001574-A	Invertase from Candida utilis		9001-57-4	Price

As a specialist in analytical chemical Products, Alfa Chemistry offers consumers a wealth of raw materials and a full range of technologies and services.

QUICK LINKS

HEADQUARTERS

Tel:

Fax:

Email: