scholarly journals An analysis of exo-polygalacturonase bioprocess in submerged and solid-state fermentation by Pleurotus ostreatus using pomelo peel powder as carbon source

Author(s):  
Kausik Majumder ◽  
Bubai Paul ◽  
Rakhi Sundas

Abstract Background As there has been an increasing trend in the effective utilization of plant and crop residues for microbial transformation into a desired product, an attempt was made to compare of exo-polygalacturonase production using logistic and Luedeking-Piret kinetic model by Pleurotus ostreatus in submerged (smf) or solid-state fermentation (ssf) using pomelo peel powder, an agro-forestry residue as carbon substrate. Results Cultures grown in submerged fermentation produced a peak of exo-polygalacturonase activity as 6160 Ul-1 on the 4th day of culture as compared with 2410 Ul-1 on the 5th day of fermentation by solid-state fermentation. The enzyme yield coefficient (YE/X) is of higher value in smf vs. ssf system (YE/X = 1.05 × 103 vs. 0.622 × 103) indicating the more efficient product yield in smf as compared with ssf. The plots derived fromλ versusζ clearly demonstrate that the secondary product destruction is higher in smf than in ssf. Conclusion P. ostreatus performs much better in submerged fermentation as compared with solid-state fermentation in respect to exo-polygalacturonase production although ssf technique produced a more thermo-stable exo-polygalacturonase in crude extract, which is highly desirable in various industrial applications.

2018 ◽  
Vol 81 (1) ◽  
Author(s):  
Halifah Pagarra ◽  
Roshanida A. Rahman ◽  
Nur Izyan Wan Azelee ◽  
Rosli Md Illias

Polygalacturonases represent an important member of pectinases group of enzymes with immense industrial applications. The activity of exo-polygalacturonase produced by Aspergillus niger was studied in solid state fermentation (SSF) using Nephrolepis biserrata leaves as substrate. Central composite design (CCD) was used to optimize four significant variables resulted from the screening process that has been initially analyzed for the production of exo-polygalacturonase which are incubation time, temperature, concentration of pectin and moisture content. The optimum exo-polygalacturonase production obtained was 54.64 U/g at 120 hours of incubation time, temperature at 340C, 5.0 g/L of pectin concentration and 75.26% of moisture content. For partial characterization of exo-polygalacturonase, the optimum temperature and pH were obtained at 50°C and pH 4.0, respectively. SDS-PAGE analysis showed that molecular weight of exo-polygalacturonase were 35 and 71 kDa. This study has revealed a significant production of exo-polygalacturonase by A. niger under SSF using cheap and easily available substrate and thus could found immense potential application in industrial sectors and biotechnology


2018 ◽  
Vol 2018 ◽  
pp. 1-10 ◽  
Author(s):  
Oliyad Jeilu Oumer ◽  
Dawit Abate

The request for enzymes in the global market is expected to rise at a fast pace in recent years. With this regard, there has been a great increase in industrial applications of pectinase owing to their significant biotechnological uses. This study was undertaken with main objectives of meeting the growing industrial demands of pectinase, by improving the yield without increasing the cost of production. In addition, this research highlights the underestimated potential of agroresidues for the production of biotechnologically important products. In this study, the maximum pectinase production attained was using wheat bran, among the tested agroresidues. The production of pectinase was improved from 10.1 ± 1.4 U/ml to 66.3 ± 1.2 U/ml in submerged fermentation whereas it was in solid state fermentation from 800.0 ± 16.2 U/g to 1272.4 ± 25.5 U/g. The maximum pectinase production was observed using YEP (submerged fermentation) and wheat bran (solid state fermentation) at initial pH of 6.5, at 37°C and by supplementing the medium with 3 mM MgSO4.7H2O.


2016 ◽  
Vol 15 (28) ◽  
pp. 1511-1519 ◽  
Author(s):  
Becker Onofre Sideney ◽  
Abatti Dirceu ◽  
Refosco Douglas ◽  
Antonio Tessaro Amarildo ◽  
Alisson Becker Onofre Jean ◽  
...  

BioResources ◽  
2021 ◽  
Vol 16 (2) ◽  
pp. 3797-3807
Author(s):  
Magdah Ganash ◽  
Tarek M. Abdel Ghany ◽  
Mohamed A. Al Abboud ◽  
Mohamed M. Alawlaqi ◽  
Husam Qanash ◽  
...  

Lignocellulolytic white-rot fungi allow the bioconversion of agricultural wastes into value-added products that are used in a myriad of applications. The aim of this work was to use corn residues (Zea mays L.) to produce valuable products under solid-state fermentation (SSF) with Pleurotus ostreatus. White-rot fungus P. ostreatus was isolated from maize silage (MS) and thereafter it was inoculated on MS as substrate and compared with maize stover (MSt) and maize cobs (MC) to determine the best lignocellulosic substrate for the production of lignocellulolytic enzymes and extracellular protein. The MS gave the highest productivity of CMCase (368.2 U/mL), FPase (170.5 U/mL), laccase (11.4 U/mL), and MnPase (6.6 U/mL). This is compared to productivity on MSt of 222 U/mL, 50.2 U/mL, 4.55 U/mL, and 2.57 U/mL, respectively; and productivity on MC at the same incubation period as 150.5 U/mL, 48.2 U/mL, 3.58 U/mL, and 2.5 U/mL, respectively. The levels of enzyme production declined with increasing incubation period after 15 and 20 days using MS and MC, respectively, as substrates. Maximum liberated extracellular protein content (754 to 878 µg/mL) was recorded using MS, while a low amount (343 to 408 µg/mL) was liberated with using MSt and MC.


2004 ◽  
Vol 47 (5) ◽  
pp. 813-819 ◽  
Author(s):  
Natalia Martin ◽  
Simone Regina de Souza ◽  
Roberto da Silva ◽  
Eleni Gomes

Pectin lyase and polygalacturonase production by newly isolated fungal strains was carried out in solid-state fermentation. Moniliella SB9 and Penicillium sp EGC5 produced polygalcturonase (PG) and pectin lyase (PL) on mixture of orange bagasse, sugar cane bagasse and wheat bran as substrate. PG and PL produced by Moniliella presented optimum activity at pH 4.5 and 10.0 and at 55 and 45°C, respectively, while these enzymes from Penicillium sp presented optimum activity at pH 4.5-5.0 and 9.0 and 40°C, respectively.


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