Production of α-amylase by Aspergillus terreus NCFT 4269.10 using pearl millet and its structural characterization
In this investigation, Aspergillus terreus NCFT4269.10 was employed in liquid static surface (LSSF) and solid state (SSF) fermentation to assess the optimal conditions for α-amylase biosynthesis. One-variable-at-a-time approach (quasi-optimum protocol) was primarily used to investigate the effect of...
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doaj-59f1e09924dd465b85d90530791737872020-11-24T23:44:26ZengFrontiers Media S.A.Frontiers in Plant Science1664-462X2016-05-01710.3389/fpls.2016.00639196883Production of α-amylase by Aspergillus terreus NCFT 4269.10 using pearl millet and its structural characterizationBIJAY KUMAR eSETHI0Arjit eJana1Prativa K. eNanda2Pradeep K. eDasMohapatra3Santi L. eSahoo4Jayanta K ePatra5Utkal UniversityVidyasagar UniversitySaila Bala Women’s CollegeVidyasagar UniversityUtkal UniversityResearch Institute of Biotechnology & Medical Converged Science, Dongguk UniversityIn this investigation, Aspergillus terreus NCFT4269.10 was employed in liquid static surface (LSSF) and solid state (SSF) fermentation to assess the optimal conditions for α-amylase biosynthesis. One-variable-at-a-time approach (quasi-optimum protocol) was primarily used to investigate the effect of each parameter on production of amylase. The maximum amylase production was achieved using pearl millet (PM) as substrate by SSF (19.19± 0.9 Ug-1) and also in presence of 1mM magnesium sulphate, 0.025% (w/v) gibberellic acid and 30 mg/100ml (w/v) of vitamin E (~ 60 fold higher production of amylase) with the initial medium pH of 7.0 and incubation at 30 ºC for 96 h. In addition, maltose, gelatin and isoleucine also influenced the α-amylase production. Amylase was purified to homogeneity with molecular mass around 15.3 kDa. The enzyme comprised of a typical secondary structure containing α-helix (12.2%), β-pleated sheet (23.6%) and β-turn (27.4%). Exploitation of PM for α-amylase production with better downstream makes it the unique enzyme for various biotechnological applications.http://journal.frontiersin.org/Journal/10.3389/fpls.2016.00639/fullsilver nanoparticlesAntibacterialantioxidantSynergisticAnticandidalWatermelon rind |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
BIJAY KUMAR eSETHI Arjit eJana Prativa K. eNanda Pradeep K. eDasMohapatra Santi L. eSahoo Jayanta K ePatra |
spellingShingle |
BIJAY KUMAR eSETHI Arjit eJana Prativa K. eNanda Pradeep K. eDasMohapatra Santi L. eSahoo Jayanta K ePatra Production of α-amylase by Aspergillus terreus NCFT 4269.10 using pearl millet and its structural characterization Frontiers in Plant Science silver nanoparticles Antibacterial antioxidant Synergistic Anticandidal Watermelon rind |
author_facet |
BIJAY KUMAR eSETHI Arjit eJana Prativa K. eNanda Pradeep K. eDasMohapatra Santi L. eSahoo Jayanta K ePatra |
author_sort |
BIJAY KUMAR eSETHI |
title |
Production of α-amylase by Aspergillus terreus NCFT 4269.10 using pearl millet and its structural characterization |
title_short |
Production of α-amylase by Aspergillus terreus NCFT 4269.10 using pearl millet and its structural characterization |
title_full |
Production of α-amylase by Aspergillus terreus NCFT 4269.10 using pearl millet and its structural characterization |
title_fullStr |
Production of α-amylase by Aspergillus terreus NCFT 4269.10 using pearl millet and its structural characterization |
title_full_unstemmed |
Production of α-amylase by Aspergillus terreus NCFT 4269.10 using pearl millet and its structural characterization |
title_sort |
production of α-amylase by aspergillus terreus ncft 4269.10 using pearl millet and its structural characterization |
publisher |
Frontiers Media S.A. |
series |
Frontiers in Plant Science |
issn |
1664-462X |
publishDate |
2016-05-01 |
description |
In this investigation, Aspergillus terreus NCFT4269.10 was employed in liquid static surface (LSSF) and solid state (SSF) fermentation to assess the optimal conditions for α-amylase biosynthesis. One-variable-at-a-time approach (quasi-optimum protocol) was primarily used to investigate the effect of each parameter on production of amylase. The maximum amylase production was achieved using pearl millet (PM) as substrate by SSF (19.19± 0.9 Ug-1) and also in presence of 1mM magnesium sulphate, 0.025% (w/v) gibberellic acid and 30 mg/100ml (w/v) of vitamin E (~ 60 fold higher production of amylase) with the initial medium pH of 7.0 and incubation at 30 ºC for 96 h. In addition, maltose, gelatin and isoleucine also influenced the α-amylase production. Amylase was purified to homogeneity with molecular mass around 15.3 kDa. The enzyme comprised of a typical secondary structure containing α-helix (12.2%), β-pleated sheet (23.6%) and β-turn (27.4%). Exploitation of PM for α-amylase production with better downstream makes it the unique enzyme for various biotechnological applications. |
topic |
silver nanoparticles Antibacterial antioxidant Synergistic Anticandidal Watermelon rind |
url |
http://journal.frontiersin.org/Journal/10.3389/fpls.2016.00639/full |
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