Bijay Kumar Sethi
Utkal University
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Featured researches published by Bijay Kumar Sethi.
Brazilian Journal of Microbiology | 2016
Bijay Kumar Sethi; Prativa Kumari Nanda; Santilata Sahoo
Enzyme production by Aspergillus terreus NCFT 4269.10 was studied under liquid static surface and solid-state fermentation using mustard oil cake as a substrate. The maximum lipase biosynthesis was observed after incubation at 30 °C for 96 h. Among the domestic oils tested, the maximum lipase biosynthesis was achieved using palm oil. The crude lipase was purified 2.56-fold to electrophoretic homogeneity, with a yield of 8.44%, and the protein had a molecular weight of 46.3 kDa as determined by SDS-PAGE. Enzyme characterization confirmed that the purified lipase was most active at pH 6.0, temperature of 50 °C, and substrate concentration of 1.5%. The enzyme was thermostable at 60 °C for 1 h, and the optimum enzyme–substrate reaction time was 30 min. Sodium dodecyl sulfate and commercial detergents did not significantly affect lipase activity during 30-min incubation at 30 °C. Among the metal ions tested, the maximum lipase activity was attained in the presence of Zn2+, followed by Mg2+ and Fe2+. Lipase activity was not significantly affected in the presence of ethylenediaminetetraacetic acid, sodium lauryl sulfate and Triton X-100. Phenylmethylsulfonyl fluoride (1 mM) and the reducing, β-mercaptoethanol significantly inhibited lipase activity. The remarkable stability in the presence of detergents, additives, inhibitors and metal ions makes this lipase unique and a potential candidate for significant biotechnological exploitation.
Frontiers in Plant Science | 2016
Bijay Kumar Sethi; Arijit Jana; Prativa Kumari Nanda; Pradeep K. DasMohapatra; Santi Lata Sahoo; Jayanta Kumar Patra
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 1 mM magnesium sulfate, 0.025% (w/v) gibberellic acid, and 30 mg/100 ml (w/v) of vitamin E (~60-fold higher production of amylase) with the initial medium pH of 7.0 and incubation at 30 °C 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.
Biofuels | 2017
Bijay Kumar Sethi; Ashutosh S. Das; Amrita Satpathy; Bikash Chandra Behera
ABSTRACT Aspergillus terreus NCFT 4269.10 was evaluated for the production of cellulase by liquid state surface fermentation (LSSF), liquid shaking fermentation (LShF) and solid state fermentation (SSF). Maximum cellulase production was observed in LSSF (344.88 ± 3.5U/ml) when banana peel (BP) was used as the substrate followed by wheat bran (WB) and sawdust (SD). The total protein content was 1160.72 ± 2.7 µg/ml when SSF was carried. It was observed that maximum biomass of A. terreus was obtained with WB (0.55 ± 0.07 g/50 ml) as compared to other substrates. Immobilized spores of A. terreus applied for fermentation study revealed maximum cellulase activity (809.38 ± 2.7 U/ml) with BP up to the second cycle and decreased thereafter. The secretion of protein content was noticed at every cycle and continued up to the fifth cycle displaying a peak at the fourth cycle (2243.83 ± 9.7 µg/ml ml) when SD was used as the substrate. It is observed that the third flask containing S. cerevisiae substrate with cellulase was able to produce the highest amount of alcohol (19.8 g/L) with high purity (1.9%) as compared to the substrate with S. cerevisiae (7.9 g/L) and co-cultivated fermentation conditions (4 g/L).
Journal of Taibah University for Science | 2016
Bijay Kumar Sethi; Arijit Jana; Prativa Kumari Nanda; Pradeep Kumar Das Mohapatra; Santi Lata Sahoo
Abstract A newly isolated fungus, Aspergillus terreus NCFT4269.10, was employed in both solid state (SSF) and liquid static surface culture (LSSC) for the production of protease using different agro-residues. Among different substrates appraised, chickling vetch peels (CVP) supported the enhanced production of protease both at LSSC and SSF (499.99 ± 11 U/ml; 5266.8 ± 202.5 U/gds, respectively). In the presence of peptone (1%, w/v), leucine (5 mM/100 ml), Fe2+ (1 mM) and riboflavin (10 mg/100 ml) with a medium pH of 5.0 incubated at 30 °C for 96 h, 3-fold higher protease production was achieved in LSSC compared with control. Fermentation kinetics studies revealed that the highest specific growth rate of A. terreus was observed in fermentation medium supplemented with riboflavin (10 mg/100 ml), i.e., 256.45 mg l−1 h−1. The growth-associated coefficient of enzyme production (α) by A. terreus was maximal when protease was produced using Fe2+. Further, the protease was purified to electrophoretic homogeneity and its molecular mass was determined as 23.8 kDa. The present strain suggests the potential utilization of inexpensive agro-residues (CVP) as medium components for the efficient industrial production using LSSC.
Cogent food & agriculture | 2016
Bijay Kumar Sethi; Prativa Kumari Nanda; Santilata Sahoo; Sangeeta Sena
Abstract α-amylase was produced by Aspergillus terreus NCFT 4269.10 using both liquid static surface (LSSF) and solid-state fermentation using pearl millet residues as substrate. The maximum production of α-amylase was noticed at 30°C incubated for 96h. The crude α-amylase was purified to electrophoretic homogeneity and characterized. Characterization of amylase confirmed that the purified α-amylase was found to be most stable at pH 5.0, 60°C temperature, and a substrate concentration of 1.25%. The enzyme was active for 40 min at 70°C with an optimum enzyme–substrate reaction time of 60 min. Amylase was compatible with all detergents tested having highest activity with Surf excel followed by Henko and Ariel. SDS and Tween 20 reduced the activity. Among the metal ions tested, the maximum α-amylase activity was attained in the presence of Ca2+, followed by Mg2+ and Mn2+. The activity of α-amylase was not considerably affected in the presence of ethylenediaminetetraacetic acid and Triton X-100. Amylase activity was accelerated in the presence of sodium lauryl sulfate and phenylmethylsulfonyl fluoride did not significantly (or slightly) affect the activity and stability. Tween 20, urea (5%), and the reducing agent, β-mercaptoethanol significantly inhibited the activity of α-amylase. Owing to its noteworthy stability in the presence of detergents, additives, inhibitors, and metal ions, this α-amylase could be an impending enzyme for significant industrial exploitations.
Annals of Microbiology | 2013
Bijay Kumar Sethi; Jyoti Ranjan Rout; Ritarani Das; Prativa Kumari Nanda; Santi Lata Sahoo
3 Biotech | 2016
Bijay Kumar Sethi; Prativa Kumari Nanda; Santilata Sahoo
International journal of pharma and bio sciences | 2013
Bijay Kumar Sethi; Prativa Kumari Nanda; Santilata Sahoo
Asian Journal of Biotechnology | 2015
Bijay Kumar Sethi; Bibekananda Panda; Santi Lata Sahoo
Journal of Microbiology and Biotechnology Research | 2017
Bijay Kumar Sethi; Satyanarayan Singh; Prativa Kumari Nanda; Santi Lata Sahoo