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

Rustiguel, Cynthia Barbosa; Oliveira, Arthur Henrique Cavalcante de; Terenzi, Héctor Francisco; Jorge, João Atı́lio; Guimarães, Luís Henrique Souza

doi:10.2225/vol14-issue2-fulltext-1

Cited by 8 publications

(9 citation statements)

References 34 publications

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“…The carbohydrate content for the invertase from C. echinulata PA3S12MM was 83.13%. This result is higher than described for enzymes from A. terreus (11.3%) (Giraldo et al, 2014), A. phoenicis (12.23%) (Rustiguel et al, 2011), A. niger (17%) (Nguyen et al, 2005),…”

Section: F I G U R Econtrasting

confidence: 61%

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: F I G U R Econtrasting

confidence: 61%

Cunninghamella echinulata PA3S12MM invertase: Biochemical characterization of a promiscuous enzyme

et al. 2021

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“…The samples were loaded on the TLC plate and placed inside the pre-saturated chamber which consisted of butanol-ethanol-water (5:3:2). The plate was air dried, dipped in the developing solution [0.2% (w/v) orcinol in a mixture of 1:9 (v/v) of H 2 SO 4 and methanol] and heated at 100 °C (Rustiguel et al 2011).…”

Section: Thin Layer Chromatographymentioning

confidence: 99%

“…There are various reported species of the genus Aspergillus such as A. niger (L'Hocine et al 2000;Nguyen et al 2005;Nadeem et al 2009), A. nidulans (Alves et al 2013), A. ochraceus (Guimaraes et al 2007), A. parasiticus (Lucca et al 2013), A. phoenicis (Rustiguel et al 2011), known to produce β-D-fructofuranosidases. The isolated microorganism was identified morphologically by lactophenol cotton blue staining as Aspergillus sp.…”

Section: Purification Studies Of β-D-fructofuranosidasementioning

confidence: 99%

“…Similarly, a purification fold of 3.11 and 9.33% of external β-D-fructofuranosidase was recovered from Fusarium solani (Bhatti et al 2006). On the other hand, β-D-fructofuranosidase from A. phoenicis (Rustiguel et al 2011) and A. ochraceus (Guimaraes et al 2007) were produced by SSF and purified by two chromatographic steps, DEAE cellulose and Sephacryl S-200 to obtain 14.46% yield and purification fold of 18.77; 24% yield and 7.1 fold, respectively. Purification of fungal β-d-fructofuranosidases in multiple steps such as three-stages (Nguyen et al 2002), four-stages (Ghosh et al 2001) or as many as eight steps of purification (L'Hocine et al 2000), reveled lesser than 30% yields and the numerous purifying stages are costly and time consuming.…”

Section: Purification Studies Of β-D-fructofuranosidasementioning

confidence: 99%

“…β-d-fructofuranosidase are reported in plants (Roitsch and Gonza ĺez 2004;Chaira et al 2010), microbial diversity such as bacteria (Yoon et al 2007;Awad et al 2013), fungi (Kurakake et al 2010;Rustiguel et al 2011;Gracida-Rodríguez et al 2014) and yeasts (Plascencia-Espinosa et al 2014;Andjelković et al 2015). β-d-fructofuranosidases are mostly studied in Saccharomyces cerevisiae strains (Rashad and Nooman 2009;Andjelković et al 2010;Veneshkumar et al 2011;Shankar et al 2013).…”

Section: Introductionmentioning

confidence: 99%

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Purification and biochemical characterization of an extracellular β-d-fructofuranosidase from Aspergillus sp.

Lincoln

2018

3 Biotech

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This study focused on the purification and characterization of an extracellular β-d-fructofuranosidase or invertase from JU12. The protein was purified by size exclusion chromatography with 5.41 fold and 10.87% recovery. The apparent molecular mass of the enzyme was estimated to be ~ 35 kDa using SDS-PAGE and confirmed by deconvoluted mass spectrometry. The fungal β-d-fructofuranosidase was suggested to be a monomer by native PAGE and zymography, and was found to be a glycoprotein possessing 68.92% carbohydrate content. The products of enzyme hydrolysis were detected by thin layer chromatography and revealed the monosaccharide units, d-glucose and d-fructose. β-d-fructofuranosidase showed enhanced activity at broad pH 4.0-9.0 and activity at a temperature range from 30 to 70 °C, while the enzyme was stable at pH 8.0 and 40 °C, respectively. The β-d-fructofuranosidase activity was lowered by metal ion inhibitors Ag and Hg whereas elevated by SDS and β-ME. The fungal β-d-fructofuranosidase was capable of hydrolyzing d-sucrose and the kinetics were determined by Lineweaver-Burk plot with of 10.17 mM and of 0.7801 µmol min. Additionally, the extracellular β-d-fructofuranosidase demonstrated tolerance to high ethanol concentrations indicating its applicability in the production of alcoholic fermentation processes.

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Industrial Approach to Invertase Production from Fruit Waste for Enhanced Efficiency and Conservation

Dokuzparmak

2024

ACS Omega

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This study investigates the commercial viability of repurposing fruit waste for enzyme production, specifically focusing on the invertase enzyme derived from Saccharomyces cerevisiae. By utilizing fruit pulp that incorporates mulberry, carob, Figure, and grape pulp as a nutrient source, it is observed that the culture medium containing carob pulp exhibits the highest invertase activity. Specifically, the invertase activity in this medium is approximately 2.5 times greater (12.90 U/mg protein) than that observed in the peptone medium (5.98 U/mg protein). The extract undergoes several purification steps, including ultrafiltration, ammonium sulfate precipitation, dialysis, and ion-exchange chromatography (purification ratio: 12.11 times, yield: 26.93%). The purified enzyme is immobilized using alginate beads, improving pH and thermal stability. The immobilized enzyme exhibits optimal activity between pH 3.50 and pH 7.00, thereby broadening the enzyme's high-activity pH range. The thermal stability of the immobilized invertase enzyme is significantly improved, especially at 65 °C. Activity studies in the presence of metal ions and certain chemicals have been conducted. The immobilized enzyme's activity increases by approximately 40% in the presence of Ca 2+ and Mg 2+ , and the immobilized enzyme maintains its activity in the presence of detergents such as SDS, Tween-20, and organic solvents like ethanol and methanol. The potential for the reuse of immobilized invertase was investigated under standard assay conditions. After 20 cycles, the immobilized enzyme was found to retain 80% of its initial activity. Overall, the study establishes the commercial potential of fruit pulp, typically discarded in fruit juice production, as a valuable source for obtaining an invertase enzyme. Furthermore, this study also aims to develop a suitable purification process for invertase in the fruit juice industry. By harnessing fruit waste and implementing innovative enzyme production strategies, industries can enhance their efficiency, reduce their environmental footprint, and optimize resource utilization.

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

Cited by 8 publications

References 34 publications

Cunninghamella echinulata PA3S12MM invertase: Biochemical characterization of a promiscuous enzyme

Cunninghamella echinulata PA3S12MM invertase: Biochemical characterization of a promiscuous enzyme

Purification and biochemical characterization of an extracellular β-d-fructofuranosidase from Aspergillus sp.

Industrial Approach to Invertase Production from Fruit Waste for Enhanced Efficiency and Conservation

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