Purification and properties of?-fructofuranosidase from Aspergillus japonicus

Abstract

β-Fructofuranosidase fromAspergillus japonicus, which produces 1-kestose (O-β-D-fructofuranosyl-(2→1)-β-D-fructofuranosyl α-D-glucopyranoside) and nystose (O-β-D-fructofuranosyl-(2→1)-β-D-fructofuranosyl-(2→1)-β-D-fructofuranosyl α-D-glucopyranoside) from sucrose, was purified to homogeneity by fractionation with calcium acetate and ammonium sulphate and chromatography with DEAE-Cellulofine and Sephadex G-200. Its molecular size was estimated to be about 304,000 Da by gel filtration. The enzyme was a glycoprotein which contained about 20% (w/w) carbohydrate. Optimum pH for the enzymatic reaction was 5.5 to 6. The enzyme was stable over a wide pH range, from pH 4 to 9. Optimum reaction temperature for the enzyme was 60 to 65°C and it was stable below 60°C. The Km value for sucrose was 0.21M. The enzyme was inhibited by metal ions, such as those of silver, lead and iron, and also byp-chloromercuribenzoate.

Production of fructooligosaccharides by β‐fructofuranosidase from Aspergillus sp 27H

“…Similar results were obtained by other researchers for Aureobasidium pullulans, 15 Aspergillus japonicus 16,17 and A niger, 12 which have already been proposed as appropriate sources of enzymes for industrial use.…”

“…However, the A Ftase reached a maximum at 60 • C and A H reached a maximum at 55 • C. The A Ftase /A H ratio suffered little variation with temperature at pH 5.5, with values between 3.5 and 5.0. Similar results were obtained by other researchers for Aureobasidium pullulans, 15 Aspergillus japonicus 16,17 and A niger, 12 which have already been proposed as appropriate sources of enzymes for industrial use.…”

Purification and characterization of β-Fructosidase with inulinase activity from Aspergillus niger - 245

“…The chromatograms also show that the peaks of inulinase and invertase activity are parallel, so much in DEAE-Sephadex A-50 as in CM-cellulose with identical values for the I/S ratio, suggesting that both activities were in a same enzymatic form or proteic molecule. Several previously published works have already demonstrated that some strains of the Aspergillus genus and yeasts produce a β-fructosidase with both activity: inulinase and invertase (Ettalibi & Baratti, 1987;Manzoni & Cavazzoni, 1988;Hayashi et al, 1992).…”

Enzymatic production of prebiotic fructo‐oligosteviol glycosides

“…The latter have been purified and characterized from higher plants, such as asparagus [3], onion [4] and Jerusalem artichoke [5], as well as various bacteria and fungi, such as Aspergillus spp. [6][7][8], Bacillus macerans [9], Schwanniomyces occidentalis [10], Candida utilis [11] and Xanthophyllomyces dendrorhous [12]. As shown in Fig.…”

“…Depending on the position of the fructosyl unit and the type of glycosidic linkage, fructans are assigned to four major categories: the graminan, inulin, levan, and neoseries fructans. Their biosynthesis is mediated by S-type and F-type FTases: 1-SST (sucrose:sucrose 1-fructosyltransferase); 6-SFT (sucrose:fructan 6-fructosyltransferase); 1-FFT (fructan:fructan 1-fructosyltransferase) and G 6 -FFT (fructan:fructan 6G-fructosyltransferase). Additionally, the concentration of total FOSGs (х) is shown.…”