The author wishes to make the following erratum to this paper []: Update due to some reporting errors in Table 2, Table 8, Table 10 and Table 12.
Due to typographical errors concerning reference [47] and [51,52], replace:
Table 2.
Approaches for improving recombinant protein production through promoter engineering.
Table 2.
Approaches for improving recombinant protein production through promoter engineering.
| Process | Modification | Performance | Improvement Factor | Reference | |
|---|---|---|---|---|---|
| Promoters | Use of several promoters (P) in A. awamori | PB2 from Acremonium chrysogenum: 0.25–2 mg/L thaumatin | - | [46] | |
| PpcbC from Penicillium chrysogenum: 0.25–2 mg/L thaumatin | |||||
| PgdhA from A. awamori: 1–9 mg/L thaumatin | |||||
| PgpdA from A. nidulans: 0.75–11 mg/L thaumatin | |||||
| Insertion of multiple copies of an activator protein-binding site from the cis-regulatory region of A. niger glaA to the new promoter in A. niger | 396.0 ± 51.5 mg/L of Vitreoscilla hemoglobin compared to 19.7 ± 4.8 mg/L from the strain with 1 copy | 20 | [45] | ||
| Use of hybrid promoters (combination of a human hERa-activated promoter (pERE), S. cerevisiae URA3 promoter and A. nidulans nirA promoter) in A. nidulans | pERE-URA-nirA + lacZ: 25 U of β-galactosidase activity/mg of protein | - | [47] | ||
| pERE-URA-RS (random stuffer-link) + lacZ: 100 U of β-galactosidase activity/mg of protein | 4 | ||||
| pERE-RS-nirA + lacZ: 1400 U of β-galactosidase activity/mg of protein [1 pM inducer (DES)] | 56 | ||||
| Use of a hemolysin-like protein promoter (Phyl) for heterologous production in A. oryzae | Reporter gene: Endoglucanase Cel B Pamy: 24.1 ± 5.5 U/mL, Phyl: 57.9 ± 17.4 U/mL | 2.4 | [48] | ||
| Reporter gene: Trichoderma endoglucanase I Pamy: 7.7 ± 3.9 U/mL, Phyl: 27.8 ± 1.3 U/mL | 3.6 | ||||
| Reporter gene: Trichoderma endoglucanase III Pamy:4.0 ± 0.6 U/mL, hyl:31.7 ± 3.3 U/mL | 7.9 | ||||
| Regulatory elements (TerR and PterA) from A. terreus terrain gene cluster for E. coli lacZ expression in A. niger | Promoter activity ~5000 mU/mg when TerR under PgpdA (No activity when TerR under the native promoter) | - | [49] | ||
| Promoter activity ~10,000 mU/mg (when TerR under PgpdA in 2 copies) | 2 | ||||
| Promoter activity ~15,000 mU/mg (when TerR under PamyB) | 3 | ||||
| A. niger α-glucosyltransferase produced under the A. niger pyruvate kinase promoter | 2000 U/mL total activity of α-glucosyltransferase compared to 600 U/mL in the wild type | 3.3 | [50] | ||
| Overexpression of the transcription factor RsmA, while the aflR promoter was inserted in front of the pslcc in A. nidulans | 60,000 U/mL of Pycnoporus sanguineus laccase compared to 4000 U/mL in the control strain | 15 | [51,52] | ||
| A novel promoter from Talaromyces emersonii (Pglucan1200) for expressing glaA in A. niger | 6000 U/mL of GlaA, enzyme activity increased by about 25% compared to 5000 U/mL in the strain with the PglaA | 1.2 | [53] | ||
| The constitutive promoter of ecm33 (Pecm33) from A. niger in A. niger | Maltose: | Pecm33 activity induced by 1.7 compared to PglaA activity that induced by 2.7 | - | [54] | |
| Glucose: | Pecm33 activity induced by 1.1 compared to PglaA activity that induced by 1.8 | ||||
| Xylose: | Pecm33 activity induced by 2 compared to PglaA activity that induced by 1.3 Increased Pecm33 activity at 37 °C | ||||
with
Table 2.
Approaches for improving recombinant protein production through promoter engineering.
Table 2.
Approaches for improving recombinant protein production through promoter engineering.
| Process | Modification | Performance | Improvement Factor | Reference | |
|---|---|---|---|---|---|
| Promoters | Use of several promoters (P) in A. awamori | PB2 from Acremonium chrysogenum: 0.25–2 mg/L thaumatin | - | [46] | |
| PpcbC from Penicillium chrysogenum: 0.25–2 mg/L thaumatin | |||||
| PgdhA from A. awamori: 1–9 mg/L thaumatin | |||||
| PgpdA from A. nidulans: 0.75–11 mg/L thaumatin | |||||
| Insertion of multiple copies of an activator protein-binding site from the cis-regulatory region of A. niger glaA to the new promoter in A. niger | 396.0 ± 51.5 mg/L of Vitreoscilla hemoglobin compared to 19.7 ± 4.8 mg/L from the strain with 1 copy | 20 | [45] | ||
| Use of hybrid promoters (combination of a human hERa-activated promoter (pERE), S. cerevisiae URA3 promoter and A. nidulans nirA promoter) in A. nidulans | pERE-RS-nirA+ lacZ: 25 U of β-galactosidase activity/mg of protein | - | [47] | ||
| pERE-URA-nirA+ lacZ: 100 U of β-galactosidase activity/mg of protein | 4 | ||||
| pERE-URA-RS + lacZ: 1400 U of β-galactosidase activity/mg of protein [1 pM inducer (DES)] | 56 | ||||
| Use of a hemolysin-like protein promoter (Phyl) for heterologous production in A. oryzae | Reporter gene: Endoglucanase Cel B Pamy: 24.1 ± 5.5 U/mL, Phyl: 57.9 ± 17.4 U/mL | 2.4 | [48] | ||
| Reporter gene: Trichoderma endoglucanase I Pamy: 7.7 ± 3.9 U/mL, Phyl: 27.8 ± 1.3 U/mL | 3.6 | ||||
| Reporter gene: Trichoderma endoglucanase III Pamy:4.0 ± 0.6 U/mL, hyl:31.7 ± 3.3 U/mL | 7.9 | ||||
| Regulatory elements (TerR and PterA) from A. terreus terrain gene cluster for E. coli lacZ expression in A. niger | Promoter activity ~5000 mU/mg when TerR under PgpdA (No activity when TerR under the native promoter) | - | [49] | ||
| Promoter activity ~10,000 mU/mg (when TerR under PgpdA in 2 copies) | 2 | ||||
| Promoter activity ~15,000 mU/mg (when TerR under PamyB) | 3 | ||||
| A. niger α-glucosyltransferase produced under the A. niger pyruvate kinase promoter | 2000 U/mL total activity of α-glucosyltransferase compared to 600 U/mL in the wild type | 3.3 | [50] | ||
| Overexpression of the transcription factor RsmA, while the aflR promoter was inserted in front of the pslcc in A. nidulans | 0.06 U/mL of Pycnoporus sanguineus laccase compared to 0.004 U/mL in the control strain | 15 | [51,52] | ||
| A novel promoter from Talaromyces emersonii (Pglucan1200) for expressing glaA in A. niger | 6000 U/mL of GlaA compared to 5000 U/mL in the strain with the PglaA | 1.2 | [53] | ||
| The constitutive promoter of ecm33 (Pecm33) from A. niger in A. niger | Maltose: | Pecm33 activity induced by 1.7 compared to PglaA activity that induced by 2.7 | - | [54] | |
| Glucose: | Pecm33 activity induced by 1.1 compared to PglaA activity that induced by 1.8 | ||||
| Xylose: | Pecm33 activity induced by 2 compared to PglaA activity that induced by 1.3 Increased Pecm33 activity at 37 °C | ||||
Due to a typographical error concerning reference [109], replace:
Table 8.
Approaches for improving recombinant protein production through engineering protein degradation pathways.
Table 8.
Approaches for improving recombinant protein production through engineering protein degradation pathways.
| Process | Modification | Performance | Improvement Factor | Reference |
|---|---|---|---|---|
| Protein degradation pathways—ERAD and Vacuole | Deletion of derA and derB in A. niger | ΔderA: 80% decrease in Tramete laccase production | 0.2 | [99] |
| - | ΔderB: 15.7% increase in Tramete laccase | 1.15 | ||
| Deletion of doaA and overexpression of sttC in A. niger | Higher GUS activity compared to parental strain (no quantitative data available) | - | [106] | |
| Disruption of Aovps10 in A. oryzae | 83.1 and 70.3 mg/L chymosin compared to 28.7 mg/L in parental strain | 3–2.5 | [108] | |
| 22.6 and 24.6 mg/L human lysozyme compared to 11.1 mg/L in parental strain | 2–2.2 | |||
| Deletion of ERAD key genes (derA, doaA, hrdC, mifA and mnsA) in A. niger | ΔderA and ΔhrdC: 2-fold increase compared to parental strain (single-copy) | 2 | [107] | |
| ΔderA: 6-fold increase compared to parental strain (multi-copy) Relative amount of intracellular GlaGus (β-glucuronidase levels) fusion protein detected in total protein extracts of strains with impaired ERAD and respective parental strain | 6 | |||
| Disruption of genes involved in autophagy in A. oryzae | ΔAoatg1: 60 mg/L chymosin | 2.3 | [109] | |
| ΔAoatg13: 37 mg/L chymosin | 1.4 | |||
| ΔAoatg4: 80 mg/L chymosin | 3.1 | |||
| ΔAoatg8: 66 mg/L chymosin | 2.5 | |||
| ΔAoatg15: Not detectable | - | |||
| Control: 26 mg/L chymosin | - |
with
Table 8.
Approaches for improving recombinant protein production through engineering protein degradation pathways.
Table 8.
Approaches for improving recombinant protein production through engineering protein degradation pathways.
| Process | Modification | Performance | Improvement Factor | Reference |
|---|---|---|---|---|
| Protein degradation pathways—ERAD and Vacuole | Deletion of derA and derB in A. niger | ΔderA: 80% decrease in Tramete laccase production | 0.2 | [99] |
| - | ΔderB: 15.7% increase in Tramete laccase | 1.15 | ||
| Deletion of doaA and overexpression of sttC in A. niger | Higher GUS activity compared to parental strain (no quantitative data available) | - | [106] | |
| Disruption of Aovps10 in A. oryzae | 83.1 and 70.3 mg/L chymosin compared to 28.7 mg/L in parental strain | 3–2.5 | [108] | |
| 22.6 and 24.6 mg/L human lysozyme compared to 11.1 mg/L in parental strain | 2–2.2 | |||
| Deletion of ERAD key genes (derA, doaA, hrdC, mifA and mnsA) in A. niger | ΔderA and ΔhrdC: 2-fold increase compared to parental strain (single-copy) | 2 | [107] | |
| ΔderA: 6-fold increase compared to parental strain (multi-copy) Relative amount of intracellular GlaGus (β-glucuronidase levels) fusion protein detected in total protein extracts of strains with impaired ERAD and respective parental strain | 6 | |||
| Disruption of genes involved in autophagy in A. oryzae | ΔAoatg1: 60 mg/L chymosin | 2.3 | [109] | |
| ΔAoatg13: 37 mg/L chymosin | 1.4 | |||
| ΔAoatg4: 80 mg/L chymosin | 3.1 | |||
| ΔAoatg8: 66 mg/L chymosin | 2.5 | |||
| ΔAoatg15: 24 mg/L chymosin | 1 | |||
| Control: 26 mg/L chymosin | - |
Due to typographical errors concerning reference [126] and [51], replace:
Table 10.
Approaches for improving recombinant protein production through disruption of protease genes.
Table 10.
Approaches for improving recombinant protein production through disruption of protease genes.
| Process | Modification | Performance | Improvement Factor | Reference |
|---|---|---|---|---|
| Proteases | Deletion of pepA in A. awamori strains | Decreased extracellular proteolytic activity compared to the wild type (immunoassay using antibodies specific for PepA, but absolute values for PepA concentration were not determined) | - | [125] |
| Deletion of pepA in A. awamori | 430 mg/L of chymosin compared to 180 mg/L in the parental strain | 2.4 | [128] | |
| Deletion of pepA in A. niger (AB1.1) | 15–20% proteolytic activity compared to the parent strain AB4.1 | - | [126] | |
| Mutation on prtT (UV irradiation) in A. niger (AB1.13) | 1–2% proteolytic activity compared to the parent strain AB4.1 | - | [126] | |
| Deletion of prtR, pepA, cpI, tppA in A. oryzae | ΔprtR/pepA/cpI: 24.23 mg/L of Acremonium cellulolyticus cellobiohydrolase | 1.2 | [133] | |
| ΔprtR/pepA/tppA: 21.30 mg/L | 1.1 | |||
| ΔprtR/cpI/tppA: 22.08 mg/L | 1.1 | |||
| ΔprtR/pepA/cpI/tppA: 19.93 mg/L compared to 19.54 mg/L in the control strains | 1.02 | |||
| Deletion of alp and Npl in A. oryzae | 1041 U/g of Candida antarctica lipase B compared to 575 U/g in the parental strains | 1.8 | [132] | |
| Deletion of various proteases in A. niger | Δdpp4: 6% increase in Tramete laccase | 1.1 | [99] | |
| Δdpp5: 15.4% increase | 1.2 | |||
| ΔpepB: 8.6% increase | 1.1 | |||
| ΔpepD: 4.8% increase | 1.0 | |||
| ΔpepF: 5.3% increase | 1.1 | |||
| ΔpepAa: 0.5% increase | 1.1 | |||
| ΔpepAb: 13.4% increase | 1.1 | |||
| ΔpepAd: 2.7% increase | 1.0 | |||
| Δdpp4/dpp5: 26.6% increase | 1.3 | |||
| Disruption of tppA and pepE in A. oryzae strains | 25.4 mg/L of human lysozyme compared to 15 mg/L in the parental strains | 1.7 | [118] | |
| Disruption of tppA, pepE, nptB, dppIV and dppV in A. oryzae | 84.4 mg/L of chymosin compared to the 63.1 mg/L in the double protease gene disruptant (ΔtppA/pepE) | 1.3 | [130] | |
| Disruption of tppA, pepE, nptB, dppIV, and dppV, alpA, pepA, AopepAa, AopepAd and cpI in A. oryzae | 109.4 mg/L of chymosin and 35.8 mg/L of human lysozyme compared to the quintuple protease gene disruptant (ΔtppA/pepE/nptB/dppIV/dppV; 84.4 mg/L and 26.5 mg/L, respectively) | 1.3 and 1.35 | [131] | |
| Deletion of prtT in A. niger | 36.3–36.7 U/mL of mL G. cingulate cutinase compared to 21.2–20.4 U/mL in the parental strain | 1.7 | [127] | |
| Stability: Cutinase activity retained at 80% over the entire 14-day incubation period, while the parental lost more than 50% of their initial activities after six days of incubation and retained negligible activity after 14 days | - | |||
| Deletion of dppV and pepA in A. nidulans | P. sanguineus laccase activity 500,000 U/mL compared to 40,000 U/mL in the control strain | 12.5 | [51] | |
| Deletion of mnn9 and pepA in A. nidulans | P. sanguineus laccase activity 300,000 U/mL compared to 40,000 U/mL in the control strain | 7.5 | [51] |
with
Table 10.
Approaches for improving recombinant protein production through disruption of protease genes.
Table 10.
Approaches for improving recombinant protein production through disruption of protease genes.
| Process | Modification | Performance | Improvement Factor | Reference |
|---|---|---|---|---|
| Proteases | Deletion of pepA in A. awamori strains | Decreased extracellular proteolytic activity compared to the wild type (immunoassay using antibodies specific for PepA, but absolute values for PepA concentration were not determined) | - | [125] |
| Deletion of pepA in A. awamori | 430 mg/L of chymosin compared to 180 mg/L in the parental strain | 2.4 | [128] | |
| Deletion of pepA in A. niger (AB1.18) | 15–20% proteolytic activity compared to the parent strain AB4.1 | - | [126] | |
| Mutation on prtT (UV irradiation) in A. niger (AB1.13) | 1–2% proteolytic activity compared to the parent strain AB4.1 | - | [126] | |
| Deletion of prtR, pepA, cpI, tppA in A. oryzae | ΔprtR/pepA/cpI: 24.23 mg/L of Acremonium cellulolyticus cellobiohydrolase | 1.2 | [133] | |
| ΔprtR/pepA/tppA: 21.30 mg/L | 1.1 | |||
| ΔprtR/cpI/tppA: 22.08 mg/L | 1.1 | |||
| ΔprtR/pepA/cpI/tppA: 19.93 mg/L compared to 19.54 mg/L in the control strains | 1.02 | |||
| Deletion of alp and Npl in A. oryzae | 1041 U/g of Candida antarctica lipase B compared to 575 U/g in the parental strains | 1.8 | [132] | |
| Deletion of various proteases in A. niger | Δdpp4: 6% increase in Tramete laccase | 1.1 | [99] | |
| Δdpp5: 15.4% increase | 1.2 | |||
| ΔpepB: 8.6% increase | 1.1 | |||
| ΔpepD: 4.8% increase | 1.0 | |||
| ΔpepF: 5.3% increase | 1.1 | |||
| ΔpepAa: 0.5% increase | 1.1 | |||
| ΔpepAb: 13.4% increase | 1.1 | |||
| ΔpepAd: 2.7% increase | 1.0 | |||
| Δdpp4/dpp5: 26.6% increase | 1.3 | |||
| Disruption of tppA and pepE in A. oryzae strains | 25.4 mg/L of human lysozyme compared to 15 mg/L in the parental strains | 1.7 | [118] | |
| Disruption of tppA, pepE, nptB, dppIV and dppV in A. oryzae | 84.4 mg/L of chymosin compared to the 63.1 mg/L in the double protease gene disruptant (ΔtppA/pepE) | 1.3 | [130] | |
| Disruption of tppA, pepE, nptB, dppIV, and dppV, alpA, pepA, AopepAa, AopepAd and cpI in A. oryzae | 109.4 mg/L of chymosin and 35.8 mg/L of human lysozyme compared to the quintuple protease gene disruptant (ΔtppA/pepE/nptB/dppIV/dppV; 84.4 mg/L and 26.5 mg/L, respectively) | 1.3 and 1.35 | [131] | |
| Deletion of prtT in A. niger | 36.3–36.7 U/mL of mL G. cingulate cutinase compared to 21.2–20.4 U/mL in the parental strain | 1.7 | [127] | |
| Stability: Cutinase activity retained at 80% over the entire 14-day incubation period, while the parental lost more than 50% of their initial activities after six days of incubation and retained negligible activity after 14 days | - | |||
| Deletion of dppV and pepA in A. nidulans | P. sanguineus laccase activity 0.5 U/mL compared to 0.04 U/mL in the control strain | 12.5 | [51] | |
| Deletion of mnn9 and pepA in A. nidulans | P. sanguineus laccase activity 0.3 U/mL compared to 0.04 U/mL in the control strain | 7.5 | [51] |
Due to a typographical error concerning reference [144], replace:
Table 12.
Approaches for improving recombinant protein production through bioprocessing modifications.
Table 12.
Approaches for improving recombinant protein production through bioprocessing modifications.
| Process | Modification | Performance | Improvement Factor | Reference |
|---|---|---|---|---|
| Fermentation conditions | Effect of growth medium and temperature on hen egg white lysozyme (HEWL) production in A. niger | 20–25 °C 8–10 mg/L HEWL while 30–37 °C 3–5 mg/L HEWL | Temperature: 2–2.6 | [141] |
| soluble starch: 8.0 mg/L HEWL | Carbon source: 1.7–2 | |||
| maltose: 4.5 mg/L HEWL | - | |||
| glucose: 4.0 mg/L HEWL | - | |||
| xylose:0.2 mg/L HEWL | - | |||
| soy milk medium: 30–60 mg/L HEWL | Rich medium: 3.8–7.5 | |||
| Effect of organic nitrogen sources on recombinant glucoamylase production in A. niger | Unsupplemented: 44 mg glucoamylase/g biomass | - | [143] | |
| L-alanine: 32 mg glucoamylase/g biomass | 0.7 | |||
| L-methionine: 26 mg glucoamylase/g | 0.6 | |||
| casamino acids, yeast extract, peptone, and gelatin: 100 mg glucoamylase/g | 2.2 | |||
| Effect of agitation intensity on recombinant amyloglucosidase (AMG) production in A. oryzae | Titer at the end of the batch phase 525 rpm: 110 U/L AMG | - | [146] | |
| 675 rpm: 230 U/L AMG | 1.6 | |||
| 825 rpm: 370 U/L AMG | 3.3 | |||
| Effects of bioprocess parameters—agitation intensity, initial glucose concentration, initial yeast extract concentration, and dissolved oxygen tension (DO)—on heterologous protein production in A. oryzae | Highest GFP yields were achieved under these conditions: agitation 400 rpm, glucose 25 g/L, yeast extract 0 g/dm3, DO 15% | - | [142] | |
| Effect of agitation intensity on recombinant glucose oxidase production in A. niger | 200 rpm: 300 mkat/L of glucose oxidase | - | [144] | |
| 500 rpm: 800 mkat/L of glucose oxidase | 2.6 | |||
| 800 rpm: 600 mkat/L of glucose oxidase | 1.3 | |||
| Effect of temperature on Pleurotus eryngii versatile peroxidase production in A. nidulans and A. niger | -A. nidulans 31 °C: 24 U/L peroxidase activity | - | [145] | |
| 28 °C: 80 U/L peroxidase activity | 3.3 | |||
| 19 °C: 466 U/L peroxidase activity | 19.4 | |||
| -A. niger 28 °C: 107 U/L peroxidase activity | - | |||
| 19 °C: 412 U/L peroxidase activity | 3.8 | |||
| Fungal morphology | Effect of raising the viscosity of the medium by addition of polyvinylpyrrolidone-PVP (transition from aggregated mycelia (pellets) to dispersed mycelia) on hen egg white lysozyme (HEWL) in A. niger | Medium with no PVP: 110 mg/L fresh and 8 mg/g dry weight of HEWL | 1.7 | [147] |
| Medium with PVP: 190 mg/L fresh and 14 mg/g dry weight of HEWL | ||||
| Effect of addition of microparticles (linked to the formation of freely dispersed mycelium) on titers of native glucoamylase (GlaA) and recombinant fructofuranosidase (FF) produced in A. niger | No microparticles: 17 U/mL GlaA and 42 U/mL FF | 3.5 GlaA 2–3.8 FF | [148] | |
| Talc microparticles: 61 U/mL GlaA and 92 U/mL FF FF production can reach up to 160 U/mL (10 g/L talc microparticles of size 6 mm) | ||||
| Effect of addition of titanate microparticles (TiSiO4, 8 mm) on titers of native glucoamylase (GlaA) and recombinant fructofuranosidase (FF) produced in A. niger | No microparticles: 19 U/mL GlaA and 40 U/mL FF | 9.5 GlaA 3.7 FF | [149] | |
| Microparticles: 190 U/mL glucoamylase and 150 U/mL fructofuranosidase | ||||
| Effect of growth type on hen egg white lysozyme (HEWL) production and protease activity in A. niger | Free suspension: 5.8 mg/g HEWL 95.3 U/g Protease activity | 1.5 | [140] | |
| Mycelial pellets: 5.0 mg/g HEWL 58.6 U/g Protease activity | 1.2 | |||
| Celite-560-immobilized cultures: 4.1 mg/g HEWL 56.3 U/g Protease activity | - |
with
Table 12.
Approaches for improving recombinant protein production through bioprocessing modifications.
Table 12.
Approaches for improving recombinant protein production through bioprocessing modifications.
| Process | Modification | Performance | Improvement Factor | Reference |
|---|---|---|---|---|
| Fermentation conditions | Effect of growth medium and temperature on hen egg white lysozyme (HEWL) production in A. niger | 20–25 °C 8–10 mg/L HEWL while 30–37 °C 3–5 mg/L HEWL | Temperature: 2–2.6 | [141] |
| soluble starch: 8.0 mg/L HEWL | Carbon source: 1.7–2 | |||
| maltose: 4.5 mg/L HEWL | - | |||
| glucose: 4.0 mg/L HEWL | - | |||
| xylose:0.2 mg/L HEWL | - | |||
| soy milk medium: 30–60 mg/L HEWL | Rich medium: 3.8–7.5 | |||
| Effect of organic nitrogen sources on recombinant glucoamylase production in A. niger | Unsupplemented: 44 mg glucoamylase/g biomass | - | [143] | |
| L-alanine: 32 mg glucoamylase/g biomass | 0.7 | |||
| L-methionine: 26 mg glucoamylase/g | 0.6 | |||
| casamino acids, yeast extract, peptone, and gelatin: 100 mg glucoamylase/g | 2.2 | |||
| Effect of agitation intensity on recombinant amyloglucosidase (AMG) production in A. oryzae | Titer at the end of the batch phase 525 rpm: 110 U/L AMG | - | [146] | |
| 675 rpm: 230 U/L AMG | 1.6 | |||
| 825 rpm: 370 U/L AMG | 3.3 | |||
| Effects of bioprocess parameters—agitation intensity, initial glucose concentration, initial yeast extract concentration, and dissolved oxygen tension (DO)—on heterologous protein production in A. oryzae | Highest GFP yields were achieved under these conditions: agitation 400 rpm, glucose 25 g/L, yeast extract 0 g/dm3, DO 15% | - | [142] | |
| Effect of agitation intensity on recombinant glucose oxidase production in A. niger | 200 rpm: 300 μkat/L of glucose oxidase | - | [144] | |
| 500 rpm: 800 μkat/L of glucose oxidase | 2.6 | |||
| 800 rpm: 600 μkat/L of glucose oxidase | 1.3 | |||
| Effect of temperature on Pleurotus eryngii versatile peroxidase production in A. nidulans and A. niger | -A. nidulans 31 °C: 24 U/L peroxidase activity | - | [145] | |
| 28 °C: 80 U/L peroxidase activity | 3.3 | |||
| 19 °C: 466 U/L peroxidase activity | 19.4 | |||
| -A. niger 28 °C: 107 U/L peroxidase activity | - | |||
| 19 °C: 412 U/L peroxidase activity | 3.8 | |||
| Fungal morphology | Effect of raising the viscosity of the medium by addition of polyvinylpyrrolidone-PVP (transition from aggregated mycelia (pellets) to dispersed mycelia) on hen egg white lysozyme (HEWL) in A. niger | Medium with no PVP: 110 mg/L fresh and 8 mg/g dry weight of HEWL | 1.7 | [147] |
| Medium with PVP: 190 mg/L fresh and 14 mg/g dry weight of HEWL | ||||
| Effect of addition of microparticles (linked to the formation of freely dispersed mycelium) on titers of native glucoamylase (GlaA) and recombinant fructofuranosidase (FF) produced in A. niger | No microparticles: 17 U/mL GlaA and 42 U/mL FF | 3.5 GlaA 2–3.8 FF | [148] | |
| Talc microparticles: 61 U/mL GlaA and 92 U/mL FF FF production can reach up to 160 U/mL (10 g/L talc microparticles of size 6 mm) | ||||
| Effect of addition of titanate microparticles (TiSiO4, 8 mm) on titers of native glucoamylase (GlaA) and recombinant fructofuranosidase (FF) produced in A. niger | No microparticles: 19 U/mL GlaA and 40 U/mL FF | 9.5 GlaA 3.7 FF | [149] | |
| Microparticles: 190 U/mL glucoamylase and 150 U/mL fructofuranosidase | ||||
| Effect of growth type on hen egg white lysozyme (HEWL) production and protease activity in A. niger | Free suspension: 5.8 mg/g HEWL 95.3 U/g Protease activity | 1.5 | [140] | |
| Mycelial pellets: 5.0 mg/g HEWL 58.6 U/g Protease activity | 1.2 | |||
| Celite-560-immobilized cultures: 4.1 mg/g HEWL 56.3 U/g Protease activity | - |
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Reference
- Ntana, F.; Mortensen, U.H.; Sarazin, C.; Figge, R. Aspergillus: A Powerful Protein Production Platform. Catalysts 2020, 10, 1064. [Google Scholar] [CrossRef]
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