Enzymes for Fructooligosaccharides Production: Achievements and Opportunities

Picazo, Brian; Flores‐Gallegos, Adriana C.; Muñiz‐Márquez, Diana B.; Flores-Maltos, Abril; Michel, Mariela R.; Rosa, Orlando de la; Rodríguez-Jasso, Rosa M.; Rodríguez‐Herrera, Raúl; Aguilar, Cristóbal N.

doi:10.1016/b978-0-12-813280-7.00018-9

Cited by 21 publications

(22 citation statements)

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“…After the three temperature treatments in the enzymatic kinetic, the 70°C treatment did not show an increment in FOS and the 50°C showed an increment only at 2 h. This could be due to the low thermostability of the enzyme, at 70°C the proteins began to denaturalize immediately and at 50°C they were denaturalized but at a lower speed. The proteins could tolerate the 50°C for a short time but when applying longer times it begins to denaturalize; instead FOS production by enzymes with fructosylating activity showed their optimal temperatures between 50 and 60°C (8). According to this behavior in both treatments, we can conclude that the enzymes produced were not thermostable.…”

Section: Discussionmentioning

confidence: 99%

“…The treatment of 30°C started producing kestose from the sucrose that aguamiel contains, as it is shown in Figure 2. The FOS production begins with kestose, and the formation of nystose was next; this mechanism is the main mechanism that a transfructosylating enzyme uses to produce FOS from sucrose (8). In accordance with the mechanism of FOS formation, the formation of fructooligosaccharides with higher DP could take more time, the production of nystose is slower than kestose, and the concentration of kestose begins to decrease as it can be observed after 10 h of the enzymatic reaction, kestose is reduced in concentration as nystose continue increasing.…”

Section: Discussionmentioning

confidence: 99%

“…Some fungi and bacteria are able to produce enzymes with FOS production capacity, but fungi are mainly used due to their capacity to produce extracellular enzymes, making the production in culture media easier. Fungi can produce FOS by different enzymatic mechanisms: fructosyltransferases, which form FOS from sucrose by transfructosylation (8); β-fructofuranosidases with hydrolytic and fructosyltransferase activity, being the hydrolytic activity preponderant during transfructosylating (9); and inulinases, enzymes that hydrolyze inulin, producing fructose monomers (exoinulinase) or/and producing shorter inulin chains or FOS (endoinulinase) (10).…”

Section: Introductionmentioning

confidence: 99%

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Production of an Enzymatic Extract From Aspergillus oryzae DIA-MF to Improve the Fructooligosaccharides Profile of Aguamiel

et al. 2019

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Aguamiel is a natural sap produced by some species of agave plants, such as Agave salmiana, A. atrovirens , or A. angustifolia . It is a product with a high concentration of fructose, glucose or sucrose, although its composition may vary depending on the season in which it is produced, and may also contain agave fructans (or agavins) or fructooligosaccharides (FOS). It has been reported that FOS can be produced by enzymes that act on sucrose or inulin, transfructosylating or hydrolyzing these materials, respectively. Due to the sugar content in aguamiel, the application of an enzymatic complex produced by Aspergillus oryzae DIA MF was carried out. This complex was characterized by 1-D electrophoresis SDS-PAGE, and its transfructosylation and hydrolysis activities were determined by HPLC. In order to determine the conditions at which the concentration of FOS in this beverage increased, kinetics were carried out at different temperatures (30, 50, and 70°C) and times (0, 1, 2, 3, 4, 5, 10, and 15 h). Finally, the antioxidant and prebiotic activities were evaluated. FOS concentration in aguamiel was increased from 1.61 ± 0.08 to 31.01 ± 3.42 g/ L after 10 h reaction at 30°C applying 10% enzymatic fraction-substrate (v/v). Antioxidant activity was highly increased (34.81–116.46 mg/eq Trolox in DPPH assay and 42.65 to 298.86 mg/eq Trolox in FRAP assay) and growth of probiotic bacteria was higher in aguamiel after the enzymatic treatment. In conclusion, after the application of the enzymatic treatment, aguamiel was enriched with FOS which improved antioxidant and prebiotic properties, so it can be used as a functional food.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Production of an Enzymatic Extract From Aspergillus oryzae DIA-MF to Improve the Fructooligosaccharides Profile of Aguamiel

et al. 2019

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“…FOS occur naturally in many plants, including onions, bananas, artichokes, tomatoes, and asparagus. They can be extracted from these sources or produced by the limited enzymatic hydrolysis of inulin, which is abundant in chicory and Jerusalem artichoke [6,7]. FOS can also be produced de novo by the enzymatic biotransformation of sucrose.…”

Section: Introductionmentioning

confidence: 99%

Development and Characterization of an Enzyme Membrane Reactor for Fructo-Oligosaccharide Production

et al. 2019

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Fructo-oligosaccharides (FOS) are linear fructans comprising 2–5 fructose units linked to a terminal glucose residue. They are widely used as food and feed additives due to their sweetness, low calorific value, and prebiotic properties. Here we describe the synthesis of FOS catalyzed by a cell-free crude enzyme solution containing recombinant fructosyltransferase (1-FFT) produced in the yeast Kluyveromyces lactis. During the enzyme catalysis, glucose accumulates as a by-product and eventually inhibits FOS production. We therefore used an enzyme membrane reactor (EMR) to achieve the continuous removal of glucose and the simultaneous replenishment of sucrose. We observed a loss of flux during the reaction with the characteristics of complete pore blocking, probably caused by a combination of proteins (enzyme molecules) and polysaccharides (FOS). Such complex fouling mechanisms must be overcome to achieve the efficient production of FOS using EMR systems.

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“…Fructooligosaccharides can be employed as functional ingredients in food products, acting as prebiotics, sugar substitutes, or fat replacers . Inulinases are versatile biocatalysts extensively used in a wide range of industrial processes for obtaining high fructose syrup and fructooligosacharides , and to a lesser extent, bioethanol , citric acid , alcohols and lactic acid . However, using the enzymes in their free form is not economically viable due to their structural instability and the loss of the enzyme during hydrolysis; moreover, released inulinase might also contaminate the products of reaction .…”

Section: Introductionmentioning

confidence: 99%

Inulinase immobilization on polyethylene glycol/polypyrrole multiwall carbon nanotubes producing a catalyst with enhanced thermal and operational stability

Temkov

Petrovski

Gjorgieva

et al. 2019

Engineering in Life Sciences

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This paper describes the development of a simple method for mixed non‐covalent and covalent bonding of partially purified inulinase on functionalized multiwall carbon nanotubes (f‐MWCNTs) with polypyrrole (PPy). The pyrrole (Py) was electrochemically polymerized on MWCNTs in order to fabricate MWCNTs/PPy nanocomposite. Two multiple forms of enzyme were bound to N‐H functional groups from PPy and ‐COO− from activated MWCNTs to yield a stable MWCNTs/PPy/PEG immobilized preparation with increased thermal stability. Fourier transform infrared (FTIR) spectroscopy and scanning electron microscopy (SEM) were used to confirm functionalization of nanoparticles and immobilization of the enzyme. The immobilization yield of 85% and optimal enzyme load of 345 μg protein onto MWCNTs was obtained. The optimum reaction conditions and kinetic parameters were established using the UV‐Vis analytical assay. The best functional performance for prepared heterogeneous catalyst has been observed at pH 3.6 and 10, and at the temperatures of 60 and 80ºC. The half‐life (t1/2) of the immobilized inulinase at 60 and 80ºC was found to be 231 and 99 min, respectively. The reusability of the immobilized formulation was evaluated based on a method in which the enzyme retained 50% of its initial activity, which occurred after the eighteenth operation cycle.

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Enzymes for Fructooligosaccharides Production: Achievements and Opportunities

Cited by 21 publications

References 81 publications

Production of an Enzymatic Extract From Aspergillus oryzae DIA-MF to Improve the Fructooligosaccharides Profile of Aguamiel

Production of an Enzymatic Extract From Aspergillus oryzae DIA-MF to Improve the Fructooligosaccharides Profile of Aguamiel

Development and Characterization of an Enzyme Membrane Reactor for Fructo-Oligosaccharide Production

Inulinase immobilization on polyethylene glycol/polypyrrole multiwall carbon nanotubes producing a catalyst with enhanced thermal and operational stability

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