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1.
Ecotoxicology ; 31(4): 565-580, 2022 May.
Article in English | MEDLINE | ID: mdl-34184169

ABSTRACT

Realising the hazardous effect of nickel on human health, microbes and plants are effectively used for bioremediation. The endophytic microorganisms have an important role in the phytoremediation of nickel using Vigna radiata. Therefore, in order to harness the potential of microbial strains, the present study was designed to examine the metal biosorption ability of endophytic bacterial strains isolated from plants growing in nickel-contaminated soil. A total of six endophytic nickel resistance bacteria were isolated from the plant Vigna radiata. The metal tolerant bacterial strains were identified following 16 S rRNA gene sequence analysis. Nickel biosorption estimation and plant growth-promoting (PGP) activities of isolated strains were performed and found high nickel biosorption efficiency of 91.3 ± 0.72% at 600 mg L-1 using Bacillus safensis an isolated endophytic strain from Vigna radiata. Furthermore, high indole acetic acid (IAA) and exopolysaccharide (EPS) production were obtained in all the strains as compared to without nickel-containing medium used as control. Moreover, the production of high EPS suggests improved biosorption ability of isolated endophytic strains. In addition, a kinetic study was also performed to evaluate different adsorptions isotherms and support the nickel biosorption ability of endophytic strains. The treatment of nickel electroplating industrial effluent was also demonstrated by isolated endophytic strains. Among six (6) strains, B. cereus showed maximum 57.2 ± 0.62% biosorption efficiency of nickel which resulted in the removal of 1003.50 ± 0.90 mg L-1 of nickel from the electroplating industry effluents containing initial 1791 ± 0.90 mg L-1 of nickel. All other strains were also capable of significant nickel biosorption from electroplating industry effluents as well. Thus, isolated endophytic nickel tolerant strains can be further used at large-scale biosorption of nickel from electroplating industry effluent.


Subject(s)
Electroplating , Nickel , Adsorption , Biodegradation, Environmental , Humans , Nickel/toxicity
2.
Bioresour Bioprocess ; 8(1): 95, 2021 Oct 05.
Article in English | MEDLINE | ID: mdl-38650192

ABSTRACT

The potential of cellulolytic enzymes has been widely studied and explored for bioconversion processes and plays a key role in various industrial applications. Cellulase, a key enzyme for cellulose-rich waste feedstock-based biorefinery, has increasing demand in various industries, e.g., paper and pulp, juice clarification, etc. Also, there has been constant progress in developing new strategies to enhance its production, such as the application of waste feedstock as the substrate for the production of individual or enzyme cocktails, process parameters control, and genetic manipulations for enzyme production with enhanced yield, efficiency, and specificity. Further, an insight into immobilization techniques has also been presented for improved reusability of cellulase, a critical factor that controls the cost of the enzyme at an industrial scale. In addition, the review also gives an insight into the status of the significant application of cellulase in the industrial sector, with its techno-economic analysis for future applications. The present review gives a complete overview of current perspectives on the production of microbial cellulases as a promising tool to develop a sustainable and greener concept for industrial applications.

3.
Int J Biol Macromol ; 122: 1191-1202, 2019 Feb 01.
Article in English | MEDLINE | ID: mdl-30223058

ABSTRACT

Xylooligosaccharides (XOS) from lignocellulosic biomass (LCB) have found widespread applications in food, feed, nutraceuticals and pharamecutical industries. Enzymatic degradation of LCB for generation of XOS have gained impetus in recent times In the present investigation an extracellular thermo-alkali stable xylanase from Aspergillus oryzae LC1 was purified by using PEG 8000/MgSO4 aqueous two-phase system and was capable of hydrolysing various agricultural residues into XOS system. Highest activity was observed using 11.3% (w/w) PEG 8000 and 22.5% (w/w) sulphate salt with maximum purification factor (13-fold), highest yield (86.8%) and partition coefficient (8.8%). The purification of the crude enzyme also resulted in decrement of ß-xylosidase activity (29.8 U/mL to 0.6 U/mL). The molecular weight of enzyme was estimated ~35 kDa. The highest residual activity was obtained with birch wood xylan as substrate with Km and Vmax of 0.2 mg/mL and 172.2 µmol min-1 mg-1 respectively. The metal ions Fe2+, Ag2+, Mg2+, Mn+ and Co+ enhanced xylanase activity while EDTA, DMSO and SDS acted as inhibitor. The effect of Fe+2 was confirmed by the circular dichroism experiment. The partially purified enzyme was capable of generating XOS i.e. xylobiose (0.68 mg/g), xylotriose (2.47 mg/g) and xylotetraose (2.29 mg/g) by direct enzymatic hydrolysis of untreated sugarcane baggase, wheat straw and wheat bran respectively.


Subject(s)
Aspergillus oryzae/enzymology , Endo-1,4-beta Xylanases/isolation & purification , Endo-1,4-beta Xylanases/metabolism , Glucuronates/chemistry , Lignin/chemistry , Oligosaccharides/chemistry , Temperature , Waste Products , Agriculture , Endo-1,4-beta Xylanases/chemistry , Enzyme Stability , Hydrogen-Ion Concentration , Kinetics , Metals/pharmacology , Molecular Weight , Substrate Specificity
4.
Int J Biol Macromol ; 125: 1042-1055, 2019 Mar 15.
Article in English | MEDLINE | ID: mdl-30562519

ABSTRACT

The white laccase was produced from Myrothecium verrucaria ITCC-8447 under submerged fermentation. The media components were optimized by response surface methodology (CCD-RSM). The nutritional components (glucose and peptone) and physical parameters (pH and temperature) were optimized by response surface methodology for enhanced laccase production by Myrothecium verrucaria ITCC-8447. The enzyme activity under optimum condition exhibited 1.45 fold increases in laccase activity. The white laccase was subjected to ion exchange chromatography with 6 fold purification. The molecular weight of white laccase was ~63-75kDa as estimated by SDS-PAGE followed by the activity staining with ABTS where green bands confirmed the presence of laccase. The enzyme was stable over an alkaline pH range of 7-9 and the temperature range of 30-40°C. The characterization of white laccase was done by CD spectra, UV-visible absorption, FTIR and XRD. The Km and Vmax values of the purified laccase were 2.5mM and1818.2µmol/min/L. The delignification capability of the white laccase was determined by reduction in Kappa number (58.8%) and Klason lignin (64.7%) of wheat straw after 12h of incubation. Further the delignification was confirmed FTIR and XRD.


Subject(s)
Fungal Proteins/chemistry , Hypocreales/enzymology , Laccase/chemistry , Lignin/chemistry , Triticum/chemistry , Enzyme Stability , Factor Analysis, Statistical , Fermentation , Fungal Proteins/isolation & purification , Fungal Proteins/metabolism , Glucose/metabolism , Glucose/pharmacology , Hydrogen-Ion Concentration , Hydrolysis , Hypocreales/chemistry , Hypocreales/drug effects , Kinetics , Laccase/isolation & purification , Laccase/metabolism , Molecular Weight , Peptones/metabolism , Peptones/pharmacology , Plant Stems/chemistry , Plant Stems/metabolism , Substrate Specificity , Temperature , Triticum/metabolism
5.
AMB Express ; 8(1): 173, 2018 Oct 17.
Article in English | MEDLINE | ID: mdl-30334113

ABSTRACT

A cellulase producing fungus Schizophyllum commune NAIMCC-F-03379 was isolated from decomposed leaf sample of Lantana camera. The nutritional components (wheat bran, magnesium sulphate and calcium chloride concentrations) and physical parameters (temperature and pH) were optimised by response surface methodology for enhanced cellulase production by S. commune NAIMCC-F-03379. The optimized medium contained: 1% (w/v) wheat bran, 0.3 g/L MgSO4, 0.8-1.0 g/L CaCl2, optimum temperature and pH were 25 °C and 5 respectively. Under optimum condition, 5.35-fold increase in CMCase and 6.62-fold increase in FPase activity was obtained as compared to un-optimized condition. Crude cellulase enzyme was subjected to different purification techniques and comparative evaluation of their efficiency was performed. The aqueous two-phase system using polyethylene glycol 8000/MnSO4 system showed maximum purification with 10.4-fold increase in activity, 79.5% yield and 0.5 partition coefficient. The cellulase enzyme obtained from S. commune NAIMCC-F-03379 has shown high stability i.e. more than 55% relative activity after 12 h of incubation over wide range of temperature (25-65 °C) and pH (3-10). The molecular weight of the cellulase enzyme was estimated as ~ 60 kDa by using sodium dodecyl sulphate-polyacrylamide electrophoresis (SDS-PAGE) and zymography. Km and Vmax value of cellulase on carboxy-methyl cellulose were obtained as 0.0909 mg/mL and 45.45 µmol/min mg respectively. Rice straw and wheat bran were subjected to hydrolysis using cellulase and cellulase-xylanase cocktail and analysed by thin layer chromatography and high performance liquid chromatography (HPLC). The HPLC analysis showed glucose concentration of 1.162 mg/mL after enzymatic hydrolysis of rice straw.

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