Multiple β-fructofuranosidases byAureobasidium pullulansDSM2404 and their roles in fructooligosaccharide production

Abstract

At least five types of beta-fructofuranosidases (FFases I, II, III, IV and V) were found in the cell wall of Aureobasidium pullulans DSM2404 grown in a sucrose medium. The fungus first catalyzed the transfructosylation of sucrose, and produced fructooligosaccharide (FOS) and glucose in the culture. FOS was then consumed together with glucose, and finally fructose was produced. In the FOS-producing period, the fungus expressed FFase I as a dominant FFase. However, in the FOS-degrading period, the levels of FFases II, III, IV and V increased. The ratios of transfructosylating activity to hydrolyzing activity by FFases I-V were 14.3, 12.1, 11.7, 1.28 and 8.11, respectively. When glucose was used as a carbon source, only FFase I showed significant activity. On the other hand, the activities of all five FFases were detected when FOS or fructose was used as a carbon source. These results suggested that the expression of FFase I was not repressed by glucose, but those of FFases II-V were strongly inhibited in the presence of glucose. It is considered that FFase I plays a key role in FOS production by this fungus, whereas FFase IV may function as a FOS-degrading enzyme with its strong hydrolyzing activity.

Biochemical properties of an extracellular β-D-fructofuranosidase II produced by Aspergillus phoenicis under Solid-Sate Fermentation using soy bran as substrate

“…Multiple β-D-fructofuranosidases forms have been reported for Aureobasidium pullulans (Yoshikawa et al 2006). Aspergillus oryzae KB was able to produce two enzymatic forms, one preferentially produced at high sucrose concentration, and another at low sucrose concentration (Kurakake et al 2008).…”

An Overview of the Recent Developments on Fructooligosaccharide Production and Applications

“…Yoshikawa et al (2006) have reported five FFase extracted from the cell wall of A. pullulans with high U t . This study also suggested that the expression of FFase I was not repressed by glucose, but those of FFases II-V were strongly inhibited in the presence of glucose, considering that FFase I played a key role in FOS production by this fungus, whereas FFase IV may function as a FOS-degrading enzyme with its strong hydrolyzing activity.…”

“…A wide variety of fungi produce FFases, but the activity ratios (U t /U h ) of their enzymes vary significantly (Sangeetha et al 2005a;Yoshikawa et al 2006). Fructosyl-transferring enzymes have been purified and characterized from higher plants, such as asparagus (Shiomi 1982), onion (Fujishima et al 2005), Jerusalem artichoke (Koops and Jonker 1994), and from different microorganisms (fungi and bacteria) such as Aspergillus niger (L'Hocine et al 2000), Aspergillus japonicus (Hayashi et al 1992), Aureobasidium pullulans (Yoshikawa et al 2006), Bacillus macerans (Park et al 2001), and Candida utilis (Chávez et al 1997). Although these proteins differ in their subunit structure, molecular weight, degree of glycosylation, chemical Food Bioprocess Technol susceptibility, and substrate specificity, they all display both hydrolytic and transfer activities (Ghazi et al 2007).…”

Production of thermostable invertases by Aspergillus caespitosus under submerged or solid state fermentation using agroindustrial residues as carbon source

“…Thermostable invertases by A. caespitosus it may be used to obtain fructooligosaccharides (FOS), used as prebiotic substance (35). Invertase is classified in the GH32 family of glycoside hydrolases, that includes over 370 members (2) and has been reported in plant (28), bacteria (34), yeast (4,12) and filamentous fungi, as Aspergillus ochraceus (11), Aspergillus niger (24), Aspergillus japonicus (7) and Thermomyces lanuginosus (6).…”