Hydrolysis of galacto-oligosaccharides in soy molasses by α -galactosidases and invertase from Aspergillus terreus

Reis, Amanda Maria Sena; Guimarães, Valéria Monteze; Ferreira, Joana Gasperazzo; Queiroz, José Humberto de; Oliveira, M. G. A.; Falkoski, Daniel Luciano; Almeida, Maíra Nicolau de; Rezende, Sebastião Tavares de

doi:10.1590/s1516-89132010000300029

Cited by 8 publications

(5 citation statements)

References 28 publications

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“…The enzymes presented activity in a broad pH range with higher activity for pH values between 3.6 and 5.6. Acid optimum pH was observed for other enzymes from A. terreus like extracellular inulinase (pH 4.0) (Coitinho et al, ) and alpha‐galactosidases (pH 5.0–5.5) (Ferreira et al, ; Reis et al, ).…”

Section: Resultsmentioning

confidence: 99%

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Purification and characterization of an invertase and a transfructosylase from Aspergillus terreus

et al. 2018

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Two intracellular invertases from Aspergillus terreus were purified and characterized. Invertase 1 has been shown maximal activity at pH 3.0 and optimum temperature at 60°C, while invertase 2 presented maximal activity at pH 4.6 and optimum temperature at 55°C. Km of invertase 1 and 2 for sucrose were 9.8 and 6.2 mM, respectively. Invertase 2 showed high thermostability presenting half‐life of 44, 14.9, and 2 hr at 40, 55, and 60°C, respectively. Gel filtration and SDS‐PAGE analysis revealed that invertase 2 has a dimeric structure composed by two monomers of 32 kDa. Fructose was a competitive inhibitor for invertase 2 presenting Ki of 61.5 mM. Besides hydrolytic activity, invertase 2 also showed transfructosylating activity producing fructooligosaccharides. The enzymes have potential to be applied in food industry since its product, inverted sugar, is used in candies and syrup production, while fructooligosacharides are prebiotics, low calorie and noncariogenic sweeteners. Practical applications Enzymes invertases hydrolyze sucrose in glucose and fructose producing inverted sugar. This product is widely used in food industry to produce jams, syrups, and fondant fillings for chocolates. Besides hydrolysis activity, some invertases can also present transfructosylating activity producing fructooligosaccharides. These oligosaccharides can act as prebiotic, providing beneficial health effects and can be used as low calorie and noncariogenic sweeteners. Aspergillus terreus produced two intracellular enzymes, one exclusively invertase, and the other, invertase and transfructosylase. The enzymes were purified and characterized in this study. This is an important step on screening new enzymes able to produce inverted sugar and fructooligosaccharides from sucrose.

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Section: Resultsmentioning

confidence: 99%

“…Many invertases has been purified and characterized from higher plants (Liu, Huang, Chang, & Sung, ) and microorganisms (Chand Bhalla, Bansuli, Thakur, Savitri, & Thakur, ; De Rezende, Feliz, & Felix, ; Reis et al, ). Intracellular transfructosylase from Aspergillus sp.…”

Section: Introductionmentioning

confidence: 99%

Purification and characterization of an invertase and a transfructosylase from Aspergillus terreus

et al. 2018

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“…α- d -Galactoside is hard to be degraded in the small intestine because humans and monogastric animals lack α-galactosidase [ 5 ]. It has been proved that the nutritive value of soy products treated by α-galactosidase alone or in combination with other enzymes is significantly improved for animal consumption [ 6 – 8 ]. Thus it’s a common practice to supplement α-galactosidase into feed to alleviate the anti-nutritional effects of RFOs.…”

Section: Introductionmentioning

confidence: 99%

Production of a Highly Protease-Resistant Fungal α-Galactosidase in Transgenic Maize Seeds for Simplified Feed Processing

et al. 2015

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Raffinose-family oligosaccharide (RFO) in soybeans is one of the major anti-nutritional factors for poultry and livestocks. α-Galactosidase is commonly supplemented into the animal feed to hydrolyze α-1,6-galactosidic bonds on the RFOs. To simplify the feed processing, a protease-resistant α-galactosidase encoding gene from Gibberella sp. strain F75, aga-F75, was modified by codon optimization and heterologously expressed in the embryos of transgentic maize driven by the embryo-specific promoter ZM-leg1A. The progenies were produced by backcrossing with the commercial inbred variety Zheng58. PCR, southern blot and western blot analysis confirmed the stable integration and tissue specific expression of the modified gene, aga-F75m, in seeds over four generations. The expression level of Aga-F75M reached up to 10,000 units per kilogram of maize seeds. In comparison with its counterpart produced in Pichia pastoris strain GS115, maize seed-derived Aga-F75M showed a lower temperature optimum (50°C) and lower stability over alkaline pH range, but better thermal stability at 60°C to 70°C and resistance to feed pelleting inactivation (80°C). This is the first report of producing α-galactosidase in transgenic plant. The study offers an effective and economic approach for direct utilization of α-galactosidase-producing maize without any purification or supplementation procedures in the feed processing.

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“…Moreover the usage of SSF for inulinase production presents the microorganism with growing conditions similar to its natural environment at low cost when compared with SmF (Singhania et al, 2010). For this purpose, different solid materials have been used as a solid substrate for SSF, such as wheat bran, rice bran, coconut oil cake, sugarcane molasses, corn steep liquor, soy molasses, Jerusalem artichoke, onion and garlic peels (Alegre et al, 2009; Ayyachamy et al, 2007; Ge and Zhang, 2005; Reis et al, 2010; Selvakumar and Pandey, 1999; Sguarezi et al, 2009; Sharma et al, 2006). It is well known that the cost and availability are significant considerations for industrial productions; therefore, selection of an appropriate substrate plays an important role in the development of enzyme production process.…”

Section: Introductionmentioning

confidence: 99%

Application of low magnetic field on inulinase production by Geotrichum candidum under solid state fermentation using leek as substrate

Canli

Kurbanoğlu

2011

Toxicol Ind Health

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This study evaluates the application of low magnetic field (LMF) on inulinase enzyme production by Geotrichum candidum under solid state fermentation (SSF) using leek as potential carbon source. First, the fermentation conditions were optimized using normal magnetic field grown microorganism. Among eight G. candidum isolates, the most effective strain called G. candidum OC-7 was selected to use in further experiments. In the second part of the study, SSF was carried out under different LMFs (4 and 7 mT). The results showed that inulinase activity was strongly affected by LMF application. The highest enzyme activity was obtained as 535.2 U/g of dry substrate (gds) by 7 mT magnetic field grown G. candidum OC-7. On the contrary, the control had only 412.1 U/gds. Consequently, the use of leek presents a great potential as an alternative carbon source for inulinase production and magnetic field treatment could effectively be used in order to enhance the enzyme production.

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Hydrolysis of galacto-oligosaccharides in soy molasses by α -galactosidases and invertase from Aspergillus terreus

Cited by 8 publications

References 28 publications

Purification and characterization of an invertase and a transfructosylase from Aspergillus terreus

Purification and characterization of an invertase and a transfructosylase from Aspergillus terreus

Production of a Highly Protease-Resistant Fungal α-Galactosidase in Transgenic Maize Seeds for Simplified Feed Processing

Application of low magnetic field on inulinase production by Geotrichum candidum under solid state fermentation using leek as substrate

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