Premium
Assay for Simultaneous Determination of β‐Cyclodextrin Glycosyltransferase (β‐CGTase) and Amylase
Author(s) -
Pócsi István,
Nógrády Noémi,
Szentirmai Attila
Publication year - 1998
Publication title -
starch ‐ stärke
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.62
H-Index - 82
eISSN - 1521-379X
pISSN - 0038-9056
DOI - 10.1002/(sici)1521-379x(199801)50:1<36::aid-star36>3.0.co;2-9
Subject(s) - starch , amylase , bacillus licheniformis , glycosyltransferase , cyclodextrin , chemistry , enzyme , reducing sugar , biochemistry , chromatography , sugar , biology , bacteria , bacillus subtilis , genetics
A new procedure was developed for the simultaneous determination of β‐cyclodextrin glycosyltransferase (β‐CGTase) and amylase activities in Bacillus macerans cultures. The new amylase assay branched off from the β‐CGTase activity measurement according to Kaneko et al. (J. Jpn. Soc. Starch Sci. 34 [1987], 45–48), included water‐soluble starch as substrate and based on the well‐characterized K 3 [Fe(CN) 6 ] reducing sugar analysis procedure. The assay had excellent within‐run and between‐run CVs, and also had an excellent correlation with the widely used 3,5‐dinitrosalicylic acid method of Bernfeld (Meth. Enzymol. 1 [1955], 149–158) using Bacillus licheniformis a ‐amylase as a model enzyme at 50°C. Neither high cyclodextrin glycosyltransferase activities nor the self‐degradation of starch interfered with the new amylase assay.