Production of Cellulase and Xylanase by &amp;lt;i&amp;gt;Aspergillus terreus&amp;lt;/i&amp;gt; KJ829487 Using Cassava Peels as Subtrates

Olanbiwoninu, Afolake Atinuke; Odunfa, S. A.

doi:10.4236/aim.2016.67050

Cited by 13 publications

(5 citation statements)

References 23 publications

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“…S. cerevisiae MK-157 produced 4.97 IU mL −1 in the first production cycle ( Table 2 ). Various moulds, including Aspergillus flavus , A. terrus , Penicillium atrovenetum and P. expansum , were found to produce only <3.7 IU mL −1 xylanase [ 29 ], which was less than the titers obtained in this study. Moulds have been reported to produce multi-enzyme outcomes that result in additional steps in the downstream production of xylanase.…”

Section: Resultscontrasting

confidence: 59%

Utilization of Corncob as an Immobilization Matrix for a Xylanolytic Yeast Strain

et al. 2023

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Immobilization of microbial cells for the production of industrially important enzymes has been reported to offer the advantages of recyclability, higher yields and cost effectiveness. The search for an appropriate matrix that is affordable and easy to prepare is a significant topic in microbial biotechnology. Here, an abundant type of agro-industrial waste—corncob—was utilized as an immobilization matrix for the production of xylanase from an indigenous yeast strain, Saccharomyces cerevisiae MK-157. This is the first report describing xylanase production from immobilized S. cerevisiae. To render the corncob matrix more porous, alkaline pretreatment was undertaken and yeast cells were immobilized on the matrix by cultivating at 30 °C for 48 h in Sabouraud dextrose broth. After incubation, the immobilized matrix was transferred to mineral salt medium containing 1% xylan and incubated at 30 °C for 24 h. Xylanase production was determined in cell-free culture supernatant and the matrix was recycled for up to seven cycles. Moreover, xylanase-mediated saccharification was carried out using sugarcane bagasse as a substrate and the release of reducing sugars was monitored. The results showed that the immobilized yeast produced 4.97 IU mL−1 xylanase in the first production cycle, indicating a >tenfold increase compared to the free cells. Xylanase production further increased to its maximum levels (9.23 IU mL−1) in the fourth production cycle. Nonetheless, the cells retained 100% productivity for up to seven cycles. The volumetric and specific productivity of xylanase were also the highest in the fourth cycle. Scanning electron microscopy images revealed the rough surface of the untreated corncob, which became more porous after alkaline pretreatment. Immobilized yeast cells were also visible on the corncob pieces. The saccharification of a natural resource—sugarcane bagasse—using xylanase preparation yielded 26 mg L−1 of reducing sugars. Therefore, it can be concluded that yeast strains can yield sufficient quantities of xylanase, allowing possible biotechnological applications. Moreover, corncob can serve as a cost-effective matrix for industrially important yeast strains.

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Section: Resultscontrasting

confidence: 59%

Utilization of Corncob as an Immobilization Matrix for a Xylanolytic Yeast Strain

et al. 2023

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“…Recently, several researchers investigated the ability of fungi to use agricultural wastes as carbon sources rich in cellulosic material, of which A. terreus species found to be a promising source of cellulose (Olanbiwoninu and Odunfa 2016;Lee et al, 2017;Ranjith et al, 2018). An isolated species of A. terreus from soil showed high levels of cellulases (Sohail et al, 2016).…”

Section: Molecular Identificationmentioning

confidence: 99%

Optimization and Characterization of Extracellular Cellulase Produced by Native Egyptian Fungal Strain

El-Baroty

Abou-Elella

Moawad

et al. 2019

Not Bot Horti Agrobo

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Since accumulation of agricultural wastes represents a huge problem, it was important to explore the available methods to help eliminate agricultural wastes safely, and simultaneously produce functional enzyme like cellulase. Six native Egyptian fungal strains were isolated, morphologically identified and screened for cellulose biodegradation potential, which was determined as endoglucanase or as carboximethylcellulase (CMCase). The most promising isolate (Aspergillus terreus) was selected for molecular characterizations based on sequencing of internal transcribed spacer (ITS). Further optimization experiments were accomplished on the selected strain. The strain with cellulolytic activity, 2.26 IU mL-1 was identified using ITS nucleotides (genes) sequences and the result confirmed that the strain is 99.8% homology with A. terreus. Then, it was submitted to GeneBank and given an accession number. Further optimization experiments revealed that 35ºC is the optimum temperature for cellulase production and raised the enzyme activity (EA) up to 3.19 IU mL-1. Out of two organic nitrogen sources; peptone at concentration 6 gL-1 was found to be the optimum nitrogen source for cellulase production with the highest activity 4 IU mL-1. Whereas, the different four carbon sources: microcellulose, corn stalks, wheat straw and rice straw showed significant differences in EA with values 11.07, 9.68, 7.87 and 3.71 IU mL-1, respectively at pH 3. The maximum EA was recorded to be within 5-7 days of incubation, dependent on type of carbon sources. The optimization of different incubation conditions raised cellulolytic activity from 2.26 IU mL-1 up to 11.18 IU mL-1. ********* In press - Online First. Article has been peer reviewed, accepted for publication and published online without pagination. It will receive pagination when the issue will be ready for publishing as a complete number (Volume 47, Issue 3, 2019). The article is searchable and citable by Digital Object Identifier (DOI). DOI link will become active after the article will be included in the complete issue. *********

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“…Hence, the potent Koji's mutant, hyper producer of thermostable endoglucanase was screened from the available mutants stock (Total = 52 variants), which was generated through gamma rays treatment of Super Koji strain (A. oryzae cmc1). Initially, seventeen (17) mutants hyper producer of CMCases were selected based on the basis of clearance zone index (CI) on the plates supplemented with 1% CMC. Afterwards, six mutants resistant to 2deoxy-D-glucose were selected having enhanced CMCase production.…”

Section: Introductionmentioning

confidence: 99%

“…Fungal cellulases are usually preferred because of higher production rate and comparatively more thermostable that can withstand the harsh industrial conditions [16]. Various fungi like Trichoderma, Aspergillus, Penicillium, Humicola, etc are industrially important producers of cellulases [17].…”

Section: Introductionmentioning

confidence: 99%

Gamma Rays Mediated Mutagenesis of Super Koji (Aspergillus oryzae) to enhance the Thermostability and Production of CMCases: Process Scale-up at Pilot Level

Zeb¹,

Rashid²,

Aleem³

et al. 2019

Preprint

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Background The β-1, 4-endoglucanase belongs to cellulases group of enzymes, which hydrolyse β-1, 4 glucosidic bonds in the naturally occurring cellulose or synthetic Carboxymethyl cellulose CMC thus also named as CMCase. Endoglucanase from Aspergillus oryzae is favoured in food and feed industries due to its GRAS (generally regarded as safe) status and for relatively stable enzymes production. Results Current report is novel as it deals with the development of super Koji strain having hyper production of thermostable CMCases. Hence, the potent Koji’s mutant, hyper producer of thermostable endoglucanase was screened from the available mutants stock (Total = 52 variants), which was generated through gamma rays treatment of Super Koji strain (A. oryzae cmc1). Initially, seventeen (17) mutants hyper producer of CMCases were selected based on the basis of clearance zone index (CI) on the plates supplemented with 1% CMC. Afterwards, six mutants resistant to 2-deoxy-D-glucose were selected having enhanced CMCase production. Mutants’ next screening was on submerged CMCase production. Potent mutant 60(5) having 60 kRad γ-rays exposure showed 3.6 folds hyper CMCase production (6.02 U ml-1). The half-life of endoglucanse produce of A. oryzae mutant 60(5) was 29.42 min and 14.8 min at 55 ⁰C and 60 ⁰C, respectively, which was 4 folds higher than the control at 60 ⁰C. The LC-MS analysis showed that A. oryzae mutant 60(5) does not produce aflatoxins. Field Emission Scanning Electron Microscopy (FESM) of mutated Koji depicted that gamma radiations enhanced the stiffness of fungal mycelia. Kinetics of CMCase production by mutant 60(5) in 10 L and 200L fermenter was as: CMCase = 913 U dl-1 & 821 U dl-1; Specific growth (µ) = 0.064 & 0.082 hours; Cell mass doubling time (td) = 10.71 & 8.42 hours; Yield coefficient with respect to cell mass (Yp/x) = 59 Ug-1 & 89 U g-1 and Specific rate of CMCase production (qp) = 3.84 Ug-1h-1 & 7.37 Ug-1h-1 respectively. Conclusion We concluded, γ-rays induced potent mutations in mutant 60(5) resulting in hyper production of thermostable endoglucanase, which can withstand harsh industrial conditions. Hence, has great potential for applications in food & feed and other industrial processes.

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Production of Cellulase and Xylanase by <i>Aspergillus terreus</i> KJ829487 Using Cassava Peels as Subtrates

Cited by 13 publications

References 23 publications

Utilization of Corncob as an Immobilization Matrix for a Xylanolytic Yeast Strain

Utilization of Corncob as an Immobilization Matrix for a Xylanolytic Yeast Strain

Optimization and Characterization of Extracellular Cellulase Produced by Native Egyptian Fungal Strain

Gamma Rays Mediated Mutagenesis of Super Koji (Aspergillus oryzae) to enhance the Thermostability and Production of CMCases: Process Scale-up at Pilot Level

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