Optimized Solid-State Fermentation Medium Enhances the Multienzymes Production from Penicillium citrinum and Aspergillus clavatus

Shruthi, B.; Achur, Rajeshwara N.

doi:10.1007/s00284-020-02036-w

Cited by 18 publications

(11 citation statements)

References 49 publications

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“…This result is in agreement with previous studies reported by Acharya et al [26] and Devanathan et al [27]. This finding was comparable to those obtained from A. clavatus [9]. However, Sulyman et al [25] reported that the maximum production of cellulase was detected at 120 h. The decreased activity obtained after this period was probably due to catabolite repression by glucose released from starch and CMC hydrolysis.…”

Section: Discussionsupporting

confidence: 93%

“…Also, Mostafa et al [8] demonstrated that the production of cellulase from fungus was obtained at 60°C. On the other hand, the amylase production from A. clavatus achieved the maximum at 30°C [9]. The temperature plays an important factor in the production of amylase and cellulase enzymes.…”

Section: Discussionmentioning

confidence: 99%

“…As we know, the production and yield of the enzyme were influenced by many factors, including temperature, pH, carbon, and nitrogen source [8,9]. The purpose of this study is the characterization of enzymatic production in different environmental conditions (incubation time, pH, and T°C), using Aspergillus niger strains, isolated from undervalued dates and processed date byproducts [5].…”

Section: Introductionmentioning

confidence: 99%

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Characterization and optimization of extracellular enzymes production by Aspergillus niger strains isolated from date by-products

Bellaouchi

Abouloifa

Rokni

et al. 2021

Journal of Genetic Engineering and Biotechnology

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Background This work aims to study the optimal conditions of the fermentation culture medium used for the production of extracellular enzymes (amylase, cellulase, lipase, and protease) from previously isolated Aspergillus niger strains in date by-products. Results The five most powerful isolates selected based on the zone of degradation formed on Petri plates by the substrate were subjected to the quantitative evaluation of their enzymatic production. All five strains showed almost similar API-ZYM profiles, with minor variations observed at the level of some specific enzyme expression. The production of cellulase and amylase was depending on pH and incubation temperatures. ASP2 strain demonstrated the high production rate of amylase (at pH 5 and 30 °C) and cellulase (at pH 6 and 30 °C) for 96 h of incubation. Conclusion The A. niger showed the ability to produce several extracellular enzymes and can be used in the valorization of different agroindustrial residues.

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Section: Discussionsupporting

confidence: 93%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Characterization and optimization of extracellular enzymes production by Aspergillus niger strains isolated from date by-products

Bellaouchi

Abouloifa

Rokni

et al. 2021

Journal of Genetic Engineering and Biotechnology

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“…Most industrial important enzymes especially -amylases are preferably isolated from microbial sources encompassing mainly the bacteria, yeasts and fungi due to the ease in genetic manipulations and bulk productions ( Lim, Oslan & Oslan, 2020 ). Therefore, native and recombinant -amylases have frequently been produced by or cloned into various microbial expression hosts including Bacillus subtilis ( Trabelsi et al, 2019a ), Enterococcus faecalis ( Meruvu, 2019 ), Aspergillus clavatus ( Shruthi, Achur & Boramuthi, 2020 ), Tepidimonas fonticaldi ( Allala et al, 2019 ), Komatagaella phaffii ( Trabelsi et al, 2019b ; Wang et al, 2019 ) and Meyerozyma guilliermondii ( Nasir et al, 2020 ).…”

Section: Survey Methodologymentioning

confidence: 99%

Native to designed: microbial α-amylases for industrial applications

Lim

Oslan

2021

PeerJ

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Background α-amylases catalyze the endo-hydrolysis of α-1,4-D-glycosidic bonds in starch into smaller moieties. While industrial processes are usually performed at harsh conditions, α-amylases from mainly the bacteria, fungi and yeasts are preferred for their stabilities (thermal, pH and oxidative) and specificities (substrate and product). Microbial α-amylases can be purified and characterized for industrial applications. While exploring novel enzymes with these properties in the nature is time-costly, the advancements in protein engineering techniques including rational design, directed evolution and others have privileged their modifications to exhibit industrially ideal traits. However, the commentary on the strategies and preferably mutated residues are lacking, hindering the design of new mutants especially for enhanced substrate specificity and oxidative stability. Thus, our review ensures wider accessibility of the previously reported experimental findings to facilitate the future engineering work. Survey methodology and objectives A traditional review approach was taken to focus on the engineering of microbial α-amylases to enhance industrially favoured characteristics. The action mechanisms of α- and β-amylases were compared to avoid any bias in the research background. This review aimed to discuss the advances in modifying microbial α-amylases via protein engineering to achieve longer half-life in high temperature, improved resistance (acidic, alkaline and oxidative) and enhanced specificities (substrate and product). Captivating results were discussed in depth, including the extended half-life at 100 °C, pH 3.5 and 10, 1.8 M hydrogen peroxide as well as enhanced substrate (65.3%) and product (42.4%) specificities. These shed light to the future microbial α-amylase engineering in achieving paramount biochemical traits ameliorations to apt in the industries. Conclusions Microbial α-amylases can be tailored for specific industrial applications through protein engineering (rational design and directed evolution). While the critical mutation points are dependent on respective enzymes, formation of disulfide bridge between cysteine residues after mutations is crucial for elevated thermostability. Amino acids conversion to basic residues was reported for enhanced acidic resistance while hydrophobic interaction resulted from mutated hydrophobic residues in carbohydrate-binding module or surface-binding sites is pivotal for improved substrate specificity. Substitution of oxidation-prone methionine residues with non-polar residues increases the enzyme oxidative stability. Hence, this review provides conceptual advances for the future microbial α-amylases designs to exhibit industrially significant characteristics. However, more attention is needed to enhance substrate specificity and oxidative stability since they are least reported.

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“…Lignocellulolytic enzymes such as cellulase and amylase are predominantly found in the forest soils of the Western Ghats. 7 Specific combinations of physicochemical and biological factors are required to maintain soil strength. Soil microorganisms and microbial processes are controlled by factors such as organic matter content, soil moisture, texture, and pH, all of which also exhibit spatial heterogeneity.…”

mentioning

confidence: 99%

Elucidation of microbial diversity and lignocellulolytic enzymes for the degradation of lignocellulosic biomass in the forest soils of Eastern and Western Ghats of Tamil Nadu, India

Valliammai

Gopal

Anandham

2020

Biofuels Bioprod Bioref

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Sustainable sources of energy are sought because of the finite nature of nonrenewable resources. Renewable energy from the lignocellulosic biomass of the forest ecosystem reduces dependency on nonrenewable resources to overcome the global energy crisis. In this study, we evaluated the physicochemical parameters of, and enzymatic activity in, 25 forest soil samples collected from Thandikudi (Western Ghats) and the Sirumalai Hills (Eastern Ghats) in Tamil Nadu, India. Soil‐sample analysis revealed that two samples obtained from the Western Ghats exhibited low and high lignocellulolytic enzyme activity, respectively, and they were considered for further study. Sample A showed low lignocellulolytic enzyme activity, whereas sample B showed high lignocellulolytic enzyme activity. The variation in the soil enzymes led us to determine the microbial communities in these two soil samples using nanopore sequencing, which targeted the V1–V9 regions of 16S rDNA. The results highlighted the positive correlation between physicochemical properties and soil enzymes. Principal component analysis revealed that, among the soil enzymes, saccharase and β‐glucosidase predominantly influenced lignocellulosic biomass degradation. The nanopore sequencing results showed that, among the microbes present, the percentage of Firmicutes was higher in soil sample B (23.03%) compared with soil sample A (14.90%). Among the bacterial genera, Bacillus was abundant in these two soil samples followed by Pseudomonas, Escherichia, and Klebsiella. The variation in the occurrence of enzymes and the availability of nutrients in the two soil samples had a positive effect on the abundance of these microbial genera. Moreover, the plentiful presence of Bacillus in soil sample B indicates the richness of lignocellulose. © 2020 Society of Chemical Industry and John Wiley & Sons, Ltd

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Optimized Solid-State Fermentation Medium Enhances the Multienzymes Production from Penicillium citrinum and Aspergillus clavatus

Cited by 18 publications

References 49 publications

Characterization and optimization of extracellular enzymes production by Aspergillus niger strains isolated from date by-products

Characterization and optimization of extracellular enzymes production by Aspergillus niger strains isolated from date by-products

Native to designed: microbial α-amylases for industrial applications

Elucidation of microbial diversity and lignocellulolytic enzymes for the degradation of lignocellulosic biomass in the forest soils of Eastern and Western Ghats of Tamil Nadu, India

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