Purification and substrate specificities of a fructanase from Kluyveromyces marxianus isolated from the fermentation process of Mezcal.
A fructanase, produced by a Kluyveromyces marxianus strain isolated during the fermentation step of the elaboration process of "Mezcal de Guerrero" was purified and biochemically characterized. The active protein was a glycosylated dimer with a molecular weight of approximately 250 kDa. The specific enzymatic activity of the protein was determined for different substrates: sucrose, inulin, Agave tequilana fructan, levan and Actilight® and compared with the activity of Fructozyme®. The hydrolysis profile of the different substrates analyzed by HPAEC-PAD showed that the enzyme has different affinities over the substrates tested with a sucrose/inulin enzymatic activity ratio (S/I) of 125. For the hydrolysis of Agave tequilana fructans, the enzyme also showed a higher enzymatic activity and specificity than Fructozyme®, which is important for its potential application in the tequila industry.
Centro de Investigación y Asistencia en Tecnología y Diseño del Estado de Jalisco, AC, Guadalajara, Jalisco, Mexico.
Javier
J
Arrizon
Sandrine
S
Morel
Anne
A
Gschaedler
Pierre
P
Monsan
D000595:Amino Acid Sequence; D004789:Enzyme Activation; D004795:Enzyme Stability; D005285:Fermentation; D006026:Glycoside Hydrolases / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D007716:Kluyveromyces / Q000201:enzymology*; D008969:Molecular Sequence Data; D013379:Substrate Specificity
D006026:Glycoside Hydrolases; C021512:levanase