Characterization of a mycelial fructosyltransferase from Aspergillus tamarii NKRC 1229 for efficient synthesis of fructooligosaccharides

Choukade, Ritumbhara; Kango, Naveen

doi:10.1016/j.foodchem.2019.02.025

Cited by 31 publications

(14 citation statements)

References 35 publications

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“…Increasing health awareness among consumers has resulted in the growing consumption of functional food products, which is expected to propel the product demand soon. Role of mycozymes in generation of health promoting prebiotic oligosaccharides and nutraceuticals has been the recent spurt of interest (Jana et al 2018 ; Choukade and Kango 2019 ; Khangwal et al 2020 ).…”

Section: Introductionmentioning

confidence: 99%

Recent Developments in Industrial Mycozymes: A Current Appraisal

Nath

Kango

2021

Mycology

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Fungi, being natural decomposers, are the most potent, ubiquitous and versatile sources of industrial enzymes. About 60% of market share of industrial enzymes is sourced from filamentous fungi and yeasts. Mycozymes (myco-fungus; zymes-enzymes) are playing a pivotal role in several industrial applications and a number of potential applications are in the offing. The field of mycozyme production, while maintaining the old traditional methods, has also witnessed a sea change due to advents in recombinant DNA technology, optimisation protocols, fermentation technology and systems biology. Consolidated bioprocessing of abundant lignocellulosic biomass and complex polysaccharides is being explored at an unprecedented pace and a number of mycozymes of diverse fungal origins are being explored using suitable platforms. The present review attempts to revisit the current status of various mycozymes, screening and production strategies and applications thereof.

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Section: Introductionmentioning

confidence: 99%

Recent Developments in Industrial Mycozymes: A Current Appraisal

Nath

Kango

2021

Mycology

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“…FTase activity was measured as described in our previous report (Choukade & Kango, 2019). In brief, 200 µl sucrose (20% w/v in 50 mM Tris‐HCl buffer, pH 7.0) was incubated with 200 µl of crude or purified FTase for 1 h at 55°C.…”

Section: Methodsmentioning

confidence: 99%

“…FTase activity was measured as described in our previous report (Choukade & Kango, 2019) and GF3). One unit of FTase was defined as the amount (µmol ml −1 ) of FOS generated per minute from sucrose biotransformation under the assay conditions.…”

Section: Ftase Assaymentioning

confidence: 99%

Purification of Aspergillus tamarii mycelial fructosyltransferase (m‐FTase), optimized FOS production, and evaluation of its anticancer potential

Choukade

Kango

2022

Journal of Food Science

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In the present study, generation of prebiotic fructooligosaccharides (FOS) using Aspergillus tamarii FTase was optimized by applying response surface methodology. Optimal FOS (251 g L −1 ) was generated at 28.4 • C, pH 7.0 and 50% (w/v) sucrose leading to 1.97-fold yield enhancement. The m-FTase was purified using ultrafiltration followed by HiTrap Q HP anion exchange chromatography resulting in 2.15-fold purified FTase with 12.76 U mg -1 specific activity. Purified FTase (75 kDa) had K m and V max values of 1049.717 mM and 2.094 µmol min -1 mg -1 , respectively. FOS incorporation led to upregulation of caspase 3, caspase 9, and Bax genes suggesting mitochondrial apoptosis activation in cancer cells. The study describes characteristics of purified FTase from A. tamarii, production optimization of FOS and unravels the role of FOS in anticancer activity against HT-29 cells.

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“…At every purification step, for the protein bands were monitored on SDS-PAGE (Laemmli 1970) and protein concentration was determined by using Bradford reagent (Bradford 1976). The zymographic analysis of the purified enzyme was done as described previously (Batista et al 2020;Choukade and Kango 2019). Further, the purified enzyme was characterized for optimum pH and temperature, pH and temperature stability.…”

Section: Purification Of Ftase From Coprophilous Fungal Isolate and Zymographymentioning

confidence: 99%

Purification and biochemical characterization of an extracellular fructosyltransferase enzyme from Aspergillus niger sp. XOBP48: implication in fructooligosaccharide production

et al. 2020

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An extracellular fructosyltransferase (Ftase) enzyme with a molar mass of ≈70 kDa from a newly isolated indigenous coprophilous fungus Aspergillus niger sp. XOBP48 is purified to homogeneity and characterized in this study. The enzyme was purified to 4.66-fold with a total yield of 15.53% and specific activity of 1219.17 U mg −1 of protein after a three-step procedure involving (NH 4 ) 2 SO 4 fractionation, dialysis and anion exchange chromatography. Ftase showed optimum activity at pH 6.0 and temperature 50 °C. Ftase exhibited over 80% residual activity at pH range of 4.0-10.0 and ≈90% residual activity at temperature range of 40-60 °C for 6 h. Metal ion inhibitors Hg 2+ and Ag + significantly inhibited Ftase activity at 1 mmol concentration. Ftase showed K m , v max and k cat values of 79.51 mmol, 45.04 µmol min −1 and 31.5 min −1 , respectively, with a catalytic efficiency (k cat /K m ) of 396 µmol −1 min −1 for the substrate sucrose. HPLC-RI experiments identified the end products of fructosyltransferase activity as monomeric glucose, 1-kestose (GF 2 ), and 1,1-kestotetraose (GF 3 ). This study evaluates the feasibility of using this purified extracellular Ftase for the enzymatic synthesis of biofunctional fructooligosaccharides.

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Characterization of a mycelial fructosyltransferase from Aspergillus tamarii NKRC 1229 for efficient synthesis of fructooligosaccharides

Cited by 31 publications

References 35 publications

Recent Developments in Industrial Mycozymes: A Current Appraisal

Recent Developments in Industrial Mycozymes: A Current Appraisal

Purification of Aspergillus tamarii mycelial fructosyltransferase (m‐FTase), optimized FOS production, and evaluation of its anticancer potential

Purification and biochemical characterization of an extracellular fructosyltransferase enzyme from Aspergillus niger sp. XOBP48: implication in fructooligosaccharide production

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