Fungal biofilm reactor improves the productivity of hydrophobin HFBII

Khalesi, Mohammadreza; Zune, Quentin; Telek, Samuel; Riveros-Galan, David; Verachtert, Hubert; Toye, Dominique; Gebruers, Kurt; Derdelinckx, Guy; Delvigne, Frank

doi:10.1016/j.bej.2014.05.001

Cited by 35 publications

(18 citation statements)

References 31 publications

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“…The large size of the fusion protein (70 kDa) could be a factor influencing its recovery in the liquid phase. In the same culture device, productivity of a 7 kDa hydrophobin in a fungal BfR is 2.54 times higher than in a submerged culture in an STR (Khalesi et al 2014). The immersed BfR works like an improved bubble column, and the absence of agitation allows for the intensification of the process and a reduction of the energy consumption in comparison with an STR.…”

Section: Discussionmentioning

confidence: 73%

A fungal biofilm reactor based on metal structured packing improves the quality of a Gla::GFP fusion protein produced by Aspergillus oryzae

Zune

Delepierre

Gofflot

et al. 2015

Appl Microbiol Biotechnol

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Section: Discussionmentioning

confidence: 73%

A fungal biofilm reactor based on metal structured packing improves the quality of a Gla::GFP fusion protein produced by Aspergillus oryzae

Zune

Delepierre

Gofflot

et al. 2015

Appl Microbiol Biotechnol

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“…Actually, HFBII is produced to protect spores when the fungi is faced with starvation condition. HFBI on the other hand is produced in order to help fungi to move from a hydrophilic environment to a hydrophobic one, and vice versa . Final purification of HFBI and HFBII using chromatography follow however the same procedure.…”

Section: Resultsmentioning

confidence: 99%

“…The resulting sample is further referred to as α L ‐HFBII. The gas flow rate of 3 L/min, ratios of the liquid height over the column height of 0.33, and glass filter G 3 (pore size = 15–40 µm) were used as the optimal separation conditions for CO 2 foam fractionation …”

Section: Methodsmentioning

confidence: 99%

Improvement of the retention of ocimene in water phase using Class II hydrophobin HFBII

Khalesi

Mandelings

Herrera‐Malaver

et al. 2015

Flavour & Fragrance J

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Hydrophobins have exceptional surface activity with potential applications for food and pharmaceutical industry. In this study, the effect of Class II hydrophobin HFBII on the retention of a volatile compound, ocimene in a water phase was investigated. We observed a negative gushing when 200 μg pure HFBII (κ-grade) and 40 μg ocimene (assay ≥ 90%) was added to 1 L sparkling water with CO 2 concentration of 7 g/L. The droplet size analysis of κ-HFBII, ocimene and the mixture of them showed that the ocimene was emulsified in a solution containing κ-HFBII. The stability of this emulsion was reduced in function of time and this effect was intensified by increasing the temperature and the presence of CO 2 . Additionally, the retention of ocimene in a HFBII rich solution was measured by SPME-GC-MS. When 0.26±0.03 mg HFBII/mL is added to ocimene solution, 43% of the original ocimene concentration (i.e. 5.9 × 10 À6 mg/mL) remained in the solution after 3 days, and 32% after 7 days. In contrast, original ocimene concentration in solutions without HFBII was only retained 20% and 14%, respectively. It showed the potential of HFBII to incorporate insoluble flavour compounds in beverages and control their release.

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“…[91] It is the same phenomenon that has been observed for other fungal metabolites such as mycotoxins and hydrophobins. [80,92] Cellulase productivity may be intensified by 80% after applying the correct feeding strategy, i.e. batch feeding, fed-batch feeding, intermittent feeding, or continuous feeding.…”

Section: The Effect Of Set-up Conditions On Cellulase Productivitymentioning

confidence: 99%

“…Many factors (e. g. vector system, codon usage, and promoter) affect the protein production and the secretion of cellulase. [66] Cultivation conditions such as substrate, [78] pH, [29] light, [79] temperatureÀtime combination of fermentation, [44] and the design of the bioreactor (either solid state or submerged fermentor), [80] may influence the morphology of fungi by inducing or prohibiting the possible stress and, thus, influence the production of the target enzyme. In the following, we will focus on the cultivation conditions to improve the yield and lower the cost of cellulase production.…”

Section: The Effect Of Set-up Conditions On Cellulase Productivitymentioning

confidence: 99%

Trichoderma reesei, a superior cellulase source for industrial applications

Keshavarz

Khalesi

2016

Biofuels

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Trichoderma reesei, a superior cellulase source for industrial applications, is a genus of filamentous fungi with an exceptional potential to produce various enzymes and proteins including cellulases, hemicellulases, and hydrophobins. Growing on easy-access low-cost substrates, as well as a broad range of products produced by T. reesei, represent this genus as the first option for bio-industries to produce required enzymes and proteins with an efficient direction of bioprocess. Recently, many researchers have made efforts to improve the yield of T. reesei cellulases using recombinant strains, optimization of the substrates, and applying the synergistic effects of co-cultivation using different microorganisms. The current findings may help industries such as biofuel producers to reduce the cost of cellulase production by up to 40%. In this review, recent advances in last five years regarding the improvement in cellulase productivity using T. reesei have been pointed out and the highlights have been summarized.

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Fungal biofilm reactor improves the productivity of hydrophobin HFBII

Cited by 35 publications

References 31 publications

A fungal biofilm reactor based on metal structured packing improves the quality of a Gla::GFP fusion protein produced by Aspergillus oryzae

A fungal biofilm reactor based on metal structured packing improves the quality of a Gla::GFP fusion protein produced by Aspergillus oryzae

Improvement of the retention of ocimene in water phase using Class II hydrophobin HFBII

Trichoderma reesei, a superior cellulase source for industrial applications

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