Immobilized, thermostable S- and F-forms of the extracellular invertase from Candida utilis can hydrolyse sucrose up to 100 degrees C

When grown on a sucrose-containing medium, Candida utilis synthesizes and secretes two invertases: one of molecular size of 280 kDa (the S-form--Slow-migrating) and a new form of Mr of 62 kDa (the F-form--Fast-migrating). Prior to immobilization, purification of S- and F-forms of invertase increased...

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Veröffentlicht in:Biotechnology letters 2002-12, Vol.24 (23), p.1993-1998
Hauptverfasser: Belcarz, A, Ginalska, G, Lobarzewski, J
Format: Artikel
Sprache:eng
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Zusammenfassung:When grown on a sucrose-containing medium, Candida utilis synthesizes and secretes two invertases: one of molecular size of 280 kDa (the S-form--Slow-migrating) and a new form of Mr of 62 kDa (the F-form--Fast-migrating). Prior to immobilization, purification of S- and F-forms of invertase increased the immobilization yield to 89-100%, in comparison with that of crude invertase preparation (52%). The immobilized purified S- and F-form of invertase remained partially active after 15 min at 100 degrees C; the F-form retained almost 30% of its maximum activity. The immobilized S-form or F-form of invertase almost completely inverted (95% hydrolysis) 60% (w/v) sucrose over 5 h continuous reaction at 80 degrees C. Moreover, at 90 degrees C the immobilized F-form hydrolysed 70% of 60% (w/v) sucrose over 5 h, while the capability of the immobilized S-form of inverting sucrose over 5 h reaction decreased from 80% to 45%.
ISSN:0141-5492
1573-6776
DOI:10.1023/A:1021138101897