Optimization of cultural and nutritional conditions for carboxymethylcellulase production by Aspergillus hortai

El-Hadi, Abeer A.; El-Nour, Salwa Abu; Hammad, Ali B. Abou; Kamel, Zeinat; Anwar, Mai

doi:10.1016/j.jrras.2013.11.003

Cited by 58 publications

(36 citation statements)

References 17 publications

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“…Optimum fermentation time may vary among different species for the enzyme production. The maximum xylanase production from Geobacillus stearothermophilus KIBGE-IB29 was reported with incubation time of 24 h; however, A. hortai showed maximum productivity of endo-1,4-β-D-glucanase after 96 h El-Hadi et al 2014). It is clearly evident from the current outcomes that bacterial culture maintained its log phase within 24 to 48 h, and any alteration in this phase depends on the environmental conditions and availability of nutrients in growth medium.…”

Section: Resultsmentioning

confidence: 69%

“…NPST-AK15 indicated maximum protease synthesis when pH of the growth medium kept at 11. However, Aspergillus hortai revealed its optimum pH at 7.0 for the maximum production of carboxymethylcellulase (CMCase) in liquid state fermentation (Ibrahim et al 2015;El-Hadi et al 2014). The initial pH of growth medium is one of the most crucial factors that affect both the bacterial cell growth and the enzyme production by altering the ionization state of nutrients (Banerjee et al 1992).…”

Section: Resultsmentioning

confidence: 99%

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Production of α-1,4-glucosidase from Bacillus licheniformis KIBGE-IB4 by utilizing sweet potato peel

Nawaz

Bibi

Karim

et al. 2016

Environ Sci Pollut Res

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In the current study, sweet potato peel (Ipomoea batatas) was observed as the most favorable substrate for the maximum synthesis of α-1,4-glucosidase among various agro-industrial residues. Bacillus licheniformis KIBGE-IB4 produced 6533.0 U ml of α-1,4-glucosidase when growth medium was supplemented with 1% dried and crushed sweet potato peel. It was evident from the results that bacterial isolate secreted 6539.0 U ml of α-1,4-glucosidase in the presence of 0.4% peptone and meat extract with 0.1% yeast extract. B. licheniformis KIBGE-IB4 released 6739.0 and 7190.0 U ml of enzyme at 40 °C and pH 7.0, respectively. An improved and cost-effective growth medium design resulted 8590.0 U ml of α-1,4-glucosidase with 1.3-fold increase as compared to initial amount from B. licheniformis KIBGE-IB4. This enzyme can be used to fulfill the accelerating demand of food and pharmaceutical industries. Further purification and immobilization of this enzyme can also enhance its utility for various commercial applications. Graphical abstract Pictorial representation of maltase production from sweet potato peel.

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Section: Resultsmentioning

confidence: 69%

Section: Resultsmentioning

confidence: 99%

Production of α-1,4-glucosidase from Bacillus licheniformis KIBGE-IB4 by utilizing sweet potato peel

Nawaz

Bibi

Karim

et al. 2016

Environ Sci Pollut Res

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“…This is similar to reports of Yazdi et al (1990), Manavalan et al (2015) and Saini et al (2015) who recorded an optimal pH of 4.5 for endoglucanase activity (crude extract) for Neurospora crassa , pH 5.0 for Penicillium oxalicum , and pH 5.0 for purified enzyme from Ganoderma lucidum , respectively. Conversely, El-Hadi et al (2013) also reported that a maximum CMCase production of 0.23 U/mL was achieved at pH 7.0 in a liquid medium and assay temperature of 37 °C for Aspergillus hortai . The effect of pH on endoglucanase production by these fungi (Fig.…”

Section: Discussionmentioning

confidence: 97%

Improved endoglucanase production and mycelial biomass of some ericoid fungi

2017

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Fungal species associated with ericaceous plant roots produce a number of enzymes and other bio-active metabolites in order to enhance survival of their host plants in natural environments. This study focussed on endoglucanase production from root associated ericoid mycorrhizal and dark septate endophytic fungal isolates. Out of the five fungal isolates screened, Leohumicola sp. (ChemRU330/PPRI 13195) had the highest relative enzyme activity and was tested along with isolates belonging to Hyloscyphaceae (EdRU083/PPRI 17284) and Leotiomycetes (EdRU002/PPRI 17261) for endoglucanase production under different pH and nutritional conditions that included: carbon sources, nitrogen sources and metal ions, at an optimum temperature of 28 °C. An optimal of pH 5.0 produced enzyme activity of 3.99, 2.18 and 4.31 (U/mg protein) for isolates EdRU083, EdRU002 and Leohumicola sp. respectively. Increased enzyme activities and improved mycelial biomass production were obtained in the presence of supplements such as potassium, sodium, glucose, maltose, cellobiose, tryptone and peptone. While NaFe-EDTA and Co2+ inhibited enzyme activity. The potential role of these fungi as a source of novel enzymes is an ongoing objective of this study.

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“…Presently, cellulases are produced from fungi, bacteria and actinomycetes, using either submerged fermentation (SmF) or solid state fermentation (SSF) on several carbon sources (Cunha et al, 2012;El-Hadi et al, 2014;Gamarra et al, 2010;Oberoi et al, 2010). When…”

Section: Enzyme Production Under Smf and Ssfmentioning

confidence: 99%

Do cultural conditions induce differential protein expression: Profiling of extracellular proteome of Aspergillus terreus CM20

Saritha

Singh

Tiwari

et al. 2016

Microbiological Research

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Optimization of cultural and nutritional conditions for carboxymethylcellulase production by Aspergillus hortai

Cited by 58 publications

References 17 publications

Production of α-1,4-glucosidase from Bacillus licheniformis KIBGE-IB4 by utilizing sweet potato peel

Production of α-1,4-glucosidase from Bacillus licheniformis KIBGE-IB4 by utilizing sweet potato peel

Improved endoglucanase production and mycelial biomass of some ericoid fungi

Do cultural conditions induce differential protein expression: Profiling of extracellular proteome of Aspergillus terreus CM20

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