Purification and partial characterization of fructosyltransferase and invertase from Aspergillus niger AS0023

L’Hocine, Lamia; Wang, Zhang; Jiang, Bo; Xu, Shicheng

doi:10.1016/s0168-1656(00)00277-7

Cited by 141 publications

(77 citation statements)

References 21 publications

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“…Many authors have reported the purification and characterization of FOS-producing enzymes from various sources and by different microorganisms (bacteria and fungi; Hayashi et al 1992;L'Hocine et al 2000;Park et al 2001;Nguyen et al 2005;Jedrzejczak-Krzepkowska et al 2011;Risso et al 2012). Although these proteins differ in their subunit structure, molecular weight, degree of glycosylation, chemical susceptibility, and substrate specificity, they all display both hydrolytic and transfer activities.…”

Section: Fos Microbial Production-transfructosylation Enzymesmentioning

confidence: 99%

“…3.2.1.26; Nguyen et al 1999;Sheu et al 2001), whereas others designate it as fructosyltransferase (FTase, EC.2.4.1.9; Yun et al 1997;Sangeetha et al 2004;Vandáková et al 2004). The latter denomination is probably due to the fact that FTase activity was originally found from the side action in the course of FFase preparation when acting on a high concentration of sucrose (Straathof et al 1986;L'Hocine et al 2000).…”

Section: Fos Microbial Production-transfructosylation Enzymesmentioning

confidence: 99%

“…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).…”

Section: Fos Microbial Production-transfructosylation Enzymesmentioning

confidence: 99%

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An Overview of the Recent Developments on Fructooligosaccharide Production and Applications

Dominguez

Rodrigues

Lima

et al. 2013

Food Bioprocess Technol

139

108

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Over the past years, many researchers have suggested that deficiencies in the diet can lead to disease states and that some diseases can be avoided through an adequate intake of relevant dietary components. Recently, a great interest in dietary modulation of the human gut has been registered. Prebiotics, such as fructooligosaccharides (FOS), play a key role in the improvement of gut microbiota balance and in individual health. FOS are generally used as components of functional foods, are generally regarded as safe (generally recognized as safe status-from the Food and Drug Administration, USA), and worth about 150€ per kilogram. Due to their nutrition-and health-relevant properties, such as moderate sweetness, low carcinogenicity, low calorimetric value, and low glycemic index, FOS have been increasingly used by the food industry. Conventionally, FOS are produced through a two-stage process that requires an enzyme production and purification step in order to proceed with the chemical reaction itself. Several studies have been conducted on the production of FOS, aiming its optimization toward the development of more efficient production processes and their potential as food ingredients. The improvement of FOS yield and productivity can be achieved by the use of different fermentative methods and different microbial sources of FOSproducing enzymes and the optimization of nutritional and culture parameter; therefore, this review focuses on the latest progresses in FOS research such as its production, functional properties, and market data.

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Section: Fos Microbial Production-transfructosylation Enzymesmentioning

confidence: 99%

Section: Fos Microbial Production-transfructosylation Enzymesmentioning

confidence: 99%

Section: Fos Microbial Production-transfructosylation Enzymesmentioning

confidence: 99%

See 1 more Smart Citation

An Overview of the Recent Developments on Fructooligosaccharide Production and Applications

Dominguez

Rodrigues

Lima

et al. 2013

Food Bioprocess Technol

139

108

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show abstract

“…Endo-inulinase hydrolyses inulin internally to produce mainly inulotriose and -tetraose (Akimoto et al, 1999), whereas exo-inulinase hydrolyses the terminal b-2,1-fructosidic bonds in both sucrose and inulin (Arand et al, 2002;Kulminskaya et al, 2003;Moriyama et al, 2003). Invertase (b-fructofuranosidase, EC 3.2.1.26), encoded by the suc1 gene (Boddy et al, 1993), hydrolyses the b-2,1-glycosidic bond in sucrose to produce fructose and glucose (L'Hocine et al, 2000). A specific b-fructosyltransferase activity (EC 2.4.1.9) without significant invertase activity has been purified from A. niger strain AS0023.…”

Section: Introductionmentioning

confidence: 99%

“…A specific b-fructosyltransferase activity (EC 2.4.1.9) without significant invertase activity has been purified from A. niger strain AS0023. This enzyme transfers fructose residues from the non-reducing terminal b-2,1-glycosidic bond in sucrose to another sucrose or inulin molecule to form kestose or higher fructo-oligosaccharides (L'Hocine et al, 2000). Unfortunately, the gene encoding this enzyme activity has not been identified and characterized yet.…”

Section: Introductionmentioning

confidence: 99%

Database mining and transcriptional analysis of genes encoding inulin-modifying enzymes of Aspergillus niger

et al. 2006

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As a soil fungus, Aspergillus niger can metabolize a wide variety of carbon sources, employing sets of enzymes able to degrade plant-derived polysaccharides. In this study the genome sequence of A. niger strain CBS 513.88 was surveyed, to analyse the gene/enzyme network involved in utilization of the plant storage polymer inulin, and of sucrose, the substrate for inulin synthesis in plants. In addition to three known activities, encoded by the genes suc1 (invertase activity; designated sucA), inuE (exo-inulinase activity) and inuA/inuB (endo-inulinase activity), two new putative invertase-like proteins were identified. These two putative proteins lack N-terminal signal sequences and therefore are expected to be intracellular enzymes. One of these two genes, designated sucB, is expressed at a low level, and its expression is up-regulated when A. niger is grown on sucrose-or inulin-containing media. Transcriptional analysis of the genes encoding the sucrose-(sucA) and inulin-hydrolysing enzymes (inuA and inuE) indicated that they are similarly regulated and all strongly induced on sucrose and inulin. Analysis of a DcreA mutant strain of A. niger revealed that expression of the extracellular inulinolytic enzymes is under control of the catabolite repressor CreA. Expression of the inulinolytic enzymes was not induced by fructose, not even in the DcreA background, indicating that fructose did not act as an inducer. Evidence is provided that sucrose, or a sucrose-derived intermediate, but not fructose, acts as an inducer for the expression of inulinolytic genes in A. niger.

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Manufacture of Prebiotic Oligosaccharides

Casci

Rastall

2012

Prebiotics: Development &Amp; Application

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Purification and partial characterization of fructosyltransferase and invertase from Aspergillus niger AS0023

Cited by 141 publications

References 21 publications

An Overview of the Recent Developments on Fructooligosaccharide Production and Applications

An Overview of the Recent Developments on Fructooligosaccharide Production and Applications

Database mining and transcriptional analysis of genes encoding inulin-modifying enzymes of Aspergillus niger

Manufacture of Prebiotic Oligosaccharides

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