Characterization of a thermo-tolerant mycelial β-fructofuranosidase from Aspergillus phoenicis under submerged fermentation using wheat bran as carbon source

Rustiguel, Cynthia Barbosa; Jorge, João Atı́lio; Guimarães, Luís Henrique Souza

doi:10.1016/j.bcab.2015.05.004

Cited by 23 publications

(14 citation statements)

References 37 publications

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“…phoenicis (Rustiguel et al, 2015) invertases. The apparent molecular mass of 89.2 kDa found in the C. echinulata PA3S12MM invertase was greater than the A. sojae (35 kDa) (Lincoln & More, 2018), A.…”

Section: Discussionmentioning

confidence: 99%

Cunninghamella echinulata PA3S12MM invertase: Biochemical characterization of a promiscuous enzyme

et al. 2021

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The Cunninghamella echinulata PA3S12MM fungus is a great producer of invertases in a growth medium supplemented by apple peels. The enzyme was purified 4.5 times after two chromatographic processes, and it presented a relative molecular mass of 89.2 kDa. The invertase reached maximum activity at pH of 6 and at 60°C, in addition to presenting stability in alkaline pH and thermal activation at 50°C. The enzymatic activity increased in the presence of Mn 2+ and dithiothreitol (DTT), while Cu 2+ and Z 2+ ions inhibited it. Also, DTT showed to protect enzymatic activity. The apparent values for K m , V máx , and K cat for the sucrose hydrolysis were, respectively, 173.8 mmol/L, 908.7 mmol/L min −1 , and 1,388.79 s −1 . The carbohydrate content was of 83.13%. The invertase presented hydrolytic activity over different types of glycosidic bonds, such as α1 ↔ 2β (sucrose), α1 → 4 (polygalacturonic acid), α1 → 4 and α1 → 2 (pectin), and α1 ↔ 1 (trehalose), indicating that the enzyme is multifunctional.Thus, the biochemical properties showed by the C. echinulata PA3S12MM suggest a broad industrial application, such as in the biomass hydrolysis or in the food industry.

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Section: Discussionmentioning

confidence: 99%

Cunninghamella echinulata PA3S12MM invertase: Biochemical characterization of a promiscuous enzyme

et al. 2021

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“…In previous works the use of the proven technology of submerged fermentation has been widely reported (Meinicke et al, 2012;Prajapati et al, 2014;Rustiguel et al, 2015;Vendruscolo et al, 2013) due to better monitoring and ease of handling. However, SSF (Solid-state fermentation) offers an alternative for low-cost enzyme production and it has different advantages such as greater yields, lower investment costs and lower energy demand (Gupta et al, 2015).…”

Section: Introductionmentioning

confidence: 99%

Potential use of soybean hulls and waste paper as supports in SSF for cellulase production by Aspergillus niger

Boggione

Belén

Bassani

et al. 2016

Biocatalysis and Agricultural Biotechnology

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Cellulase has by vast applications in the biofuel, pulp and paper, detergent and textile industries. The three components of the enzyme complex (endoglucanase, exoglucanase and β-glucosidase) can effectively depolymerize the cellulose chains in lignocellulosic substrate. Solid-state fermentation (SSF) by fungi is a preferable production route for cellulase because of its low cost, among other advantages. This work describes the cellulase production by Aspergillus niger NRRL3 grown on SSF. SSF was carried out on soybean hulls and waste paper as supports. The effect of the support on cellulase production was assessed under a completely randomized factorial design. The support-time interaction was significant for all the variables studied. Both materials were characterized in terms of water absorption index and critical humidity point. Samples of culture were analyzed with scanning electron microscopy (SEM) to study spores and fungal growth. Maximum endoglucanase activity was found at 96 h using soybean hulls as support (5914.29 U L-1), being four times higher than that obtained using waste paper at the same fermentation time. The exoglucanase activity in soybean hulls was maximal at 96 h (4551.19 U L-1), being 9.6 times higher than that obtained in waste paper at the same time. The maximum β-glucosidase activity in soybean hulls (984.01 U L-1) was reached at 96 h, being 1.7 times greater than that obtained in waste paper. Besides, the use of soybean hulls provided high volumetric productivities at shorter times, which may decrease production costs considering a scaled process.

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“…The maximal activity was obtained at 60°C and pH 5.0, unlike the enzyme from Aspergillus versicolor , whose maximal activity was obtained at 55°C and pH 6.0 (Dapper et al, ). Another fungal β‐D‐fructofuranosidase also exhibited maximal activity at 60°C similar to that of the enzyme produced by Aspergillus phoenicis (Rustiguel et al, ). In the production of FOS using β‐D‐fructofuranosidase, enzyme stability is an important aspect to be considered because synthesis of the short‐chain oligosaccharides occurs from few hours to more than 96 hr (Dominguez et al, ).…”

Section: Discussionmentioning

confidence: 67%

Production of short‐chain fructooligosaccharides (scFOS) using extracellular β‐D‐fructofuranosidase produced byAspergillus thermomutatus

Todero

Vargas-Rechia

Guimarães³

2019

J Food Biochem

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Aspergillus thermomutatus produces an extracellular β‐D‐fructofuranosidase when cultured in Khanna medium with sucrose as additional carbon source at 30°C under agitation for 72 hr. Addition of glucose and fructose in the culture medium affected the production of the enzyme negatively. The optimum hydrolytic activity was achieved at 60°C and pH 5.0, with half‐life (T50) of 30 hr at 50°C and 62% of its activity maintained at pH 5.0 for 48 hr. The extracellular extract containing β‐D‐fructofuranosidase was effective in producing fructooligosaccharides (FOS), mainly 1‐kestose. The highest concentration of FOS was obtained at 30°C and 60°C, indicating the existence of at least two enzymes with transfructosylating activity. At 30°C, the maximal FOS concentration was obtained from 48 to 72 hr, while at 60°C, it was achieved only at 72 hr. The best production of FOS (86.7 g/L) was obtained using 500 g/L sucrose as substrate. Practical application Fructooligosaccharides (FOS) are linear oligomers of fructose units with important applications in the food industry as sweetening agents and biopreservatives. Due to the presence of β‐glycosidic bonds, they cannot be hydrolyzed by human enzymes, allowing the use of FOS‐containing products by diabetics. FOS used in the preparation of dairy products imparts humectancy to soft baked products, lowers the freezing point of frozen desserts, provides crispness to low‐fat cookies, and provides many other advantages. Diets containing FOS can reduce the levels of triglycerides and cholesterol and improve the absorption of ions, such as Ca2+ and Mg2+. FOS also exhibit bifidogenic effect on Bifidobacterium and Lactobacillus strains in the colon. Industrially, FOS is produced during the transfructosylation reaction of sucrose catalyzed by β‐D‐fructofuranosidase. Identifying new sources of β‐D‐fructofuranosidase is an important challenge to meet its industrial demand.

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Characterization of a thermo-tolerant mycelial β-fructofuranosidase from Aspergillus phoenicis under submerged fermentation using wheat bran as carbon source

Cited by 23 publications

References 37 publications

Cunninghamella echinulata PA3S12MM invertase: Biochemical characterization of a promiscuous enzyme

Cunninghamella echinulata PA3S12MM invertase: Biochemical characterization of a promiscuous enzyme

Potential use of soybean hulls and waste paper as supports in SSF for cellulase production by Aspergillus niger

Production of short‐chain fructooligosaccharides (scFOS) using extracellular β‐D‐fructofuranosidase produced byAspergillus thermomutatus

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