Ideal Feedstock and Fermentation Process Improvements for the Production of Lignocellulolytic Enzymes
Abstract
:1. Introduction
2. Lignocellulosic Hydrolytic Enzymes
2.1. Cellulases
2.2. Hemicellulases
2.3. Lignases
3. Applications of Lignocellulolytic Enzymes
4. Characteristics of an Ideal Feedstock
5. Feedstocks for Lignocellulolytic Enzyme Production
6. Pretreatment of Feedstock for Lignocellulolytic Enzyme Production
- The pretreatment method should produce higher amounts of molecular entities for any specific product. For example, in the case of bioethanol production, the main ingredient required for microbial species is glucose or other monosaccharides which are to be converted into ethanol. Acid hydrolysis is one of the chemical methods that can produce higher amounts of simple sugars as compared to other methods [100]. On the other hand, if the final output is the production of lignocellulolytic enzymes such as cellulase, then the presence of reactive cellulosic fibers is required [101]. The physical pretreatment methods are usually employed to remove the lignin barrier so that cellulose and hemicellulose are available for subsequent biochemical reactions.
- The pretreatment method should not degrade the monosaccharides if they are the final product of the pretreatment. Some methods such as acid hydrolysis can degrade the pentoses and hexoses further into furfurals and Trihalomethanes (THMs), which may have an inhibitory effect on fungal activity [100].
- The pretreatment method should also not release any other type of compounds that can inhibit the growth of the microbial species, which are to be employed for the end-use of the lignocellulosic biomass. In this regard, all pretreatment methods should be checked and optimized according to the end-use of the products [102].
- The size and specifications of the pretreatment reactors should also be considered before employing a specific pretreatment method. For example, most of the acid hydrolysis reactions require high temperature and pressure (such as in an autoclave).
- The physical state of the pretreatment output also plays an important role in the determination of a suitable method. For example, if the liquid medium is required for the microbial or any other biochemical reaction, then the presence of solid residues at the end of the pretreatment procedure should be minimal.
- Simplicity of the pretreatment procedure is also required for setting up the reaction at different scales.
- The characteristics of the pretreatment feedstocks should also be taken into account before selecting a specific type of feedstock. For example, in the case of the sugarcane bagasse, chemical pretreatment methods along with steam or liquid hot water can be employed because it does not have high amounts of proteins or lipids. However, if the feedstock has high contents of proteins and lipids, such as distillers dried grains with solubles (DDGS), there is a high chance that such molecular components will also be degraded by the severe pretreatment conditions.
7. Microbial Production of Lignocellulolytic Enzymes
7.1. Modes of Fermentation for Lignocellulolytic Enzyme Production
7.2. Fermentation Enhancement Strategies
8. Challenges of Enzyme Production
9. Conclusions and Future Perspective
Author Contributions
Funding
Institutional Review Board Statement
Informed Consent Statement
Data Availability Statement
Acknowledgments
Conflicts of Interest
References
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Enzyme | Type | Enzyme Commission (EC) Number | Activity-Characteristics | Application Areas | References |
---|---|---|---|---|---|
Cellulases | Endo-β-glucanase | 3.2.1.4 | Hydrolysis of 1–3 or 1–4 bonds in the beta-D-glucans within the chain | Cereal grains; polishing; feed supplements | [12,13] |
β-Glucosidase | 3.2.1.21 | Hydrolysis from non-reducing end | Flavor enhancement; biofuel industry | [12,14] | |
Exoglucanases | 3.2.1.91 | reducing or non-reducing end creating cellobiose | Food, pulp and paper industry | [12,15] | |
Hemicellulases | Endo-β-1,4-xylanase | 3.2.1.8 | β-1,4 bonds within Xylan chains | Food industry | [16,17] |
1,4-β-Xylosidase | 3.2.1.37 | Hydrolysis from non-reducing end in β-D-Xylan | Food industry | [17,18] | |
Endo-1,4-β-mannosidase | 3.2.1.78 | β-1,4 bonds within mannan chains | Delignification in pulp industry | [17,19] | |
1,2-α-Mannosidase | 3.2.1.113 | Removal of terminal alpha-D-mannose residues | Delignification in pulp industry | [17,20] | |
β-Mannosidase | 3.2.1.25 | Hydrolysis from nonreducing end to form d-mannose residues | Delignification in pulp industry | [17,21] | |
α-Galactosidase | 3.2.1.22 | Hydrolysis of α-galactoglucomannan | Guar gum digestion | [17,22] | |
β-Galactosidase | 3.2.1.23 | Hydrolysis of β-galactoglucomannan | Medicine; guar gum digestion | [17,22] | |
α-L-Arabinofuranosidase | 3.2.1.55 | Hydrolysis of arabinoxylan and arabinoglucoronoxylan | Feed industry and baking | [17,22] | |
α-Glucuronidase | 3.2.1.139 | Hydrolysis of arabinoglucoronoxylan | Food industry | [22,23] | |
Acetyl esterase | 3.1.1.6 | Hydrolysis of the ester bond between arabinose and ferulic acid (Lignin) | Cider clarification | [17,22] | |
Acetyl xylan esterase | 3.1.1.72 | Cleaving of Acetyl groups in hemicellulose | Cider clarification | [17,22] | |
Lignin modifying enzymes (LMEs) | Lignin peroxidase | 1.11.1.14 | Oxidoreductase | Waste treatment | [24] |
Manganese peroxidase | 1.11.1.13 | Oxidoreductase | Wastewater treatment in the production of synthetic dyes | [25] | |
Phenoloxidases | 1.10.3.2 | Multicopper oxidases | Bioremediation | [26] | |
Hybrid peroxidase | 1.11.1.16 | Oxidoreductase | Industrial waste treatment | [27] |
Year | Feedstock Used | Composition of Enzyme | Maximum Enzyme Produced | Units | References |
---|---|---|---|---|---|
1970–1979 | Feedlot waste | Cellulase and hemicellulase complexes | 0.4 enzyme cocktail | FPU/g/mL | [55] |
Ball-milled Populus tremuloides | Cellulase complexes | 1.5 enzyme cocktail | U/mL | [56] | |
Wheat straw, sprouts, malt and corn cobs | Cellulase and hemicellulase complexes | 29.69 enzyme cocktail | mg sugar/mL media | [57] | |
Sugar cane bagasse | Cellulases | 48.1 enzyme cocktail | % degradation of feedstock | [58] | |
1980–1989 | Tamarind kernel polysaccharide (TKP) | Cellulases, hemicellulases, β-glucosidase and β -xylosidase | N/A | N/A | [59] |
Kallar grass | CMCase and Xylanase | 3.8 CMCase 16.0 Xylanase | IU/mL | [60] | |
Hemicellulose substrates and bagasse | Xylanase and xylosidase | 1.5 xylanase 0.08 β-xylosidase | U/mL | [61] | |
Wheat bran, rice straw | β-d-glucosidase, d-xylanase | 60 Β-d-glucosidase, 740 d-xylanase | U/g | [62] | |
Kallar grass | CMCase, avicelase, xylanase, β -glucosidase and β -xylosidase | 3.2 CMCase | IU/mL | [63] | |
1990–1999 | Corn cobs, rice hulls and melonseed shells | Cellulase and hemicellulase cocktails | 20 enzyme cocktail | % yield | [64] |
Corn Stover | Cellulase and hemicellulase cocktails | 0.7 FPA | nmol/mL/s | [65] | |
Rice straw | Cellulases and xylanases | 9.7 FPA cellulase 9100 Xylanase | IU/l/h U/g | [66] | |
Sweet sorghum silage | Cellulases and xylanases | 4 Cellulase 180 xylanase | IU/g | [67] | |
Corn fiber | Cellulase and Xylanase | 3.4 cellulase 3.7 Xylanase | U/cm3 | [68] | |
Bagasse | Cellulase and β-glucosidase | 18.7 cellulase 38.6 β-glucosidase | IU/g | [69] | |
Wood, straw | Cellulase | 7–18 | FPU/mL | [70] | |
Barley and Wheat Straw | Xylanase, glucosidase, xylosidase, esterase and arabinofuranosidase | 0.16 cellobiase 1.4 xylanase | µmol/mL/min | [71] | |
Orange peels | Cellulase, xylanase, pectinase | 3.39 cellulase 3.33 xylanase | U/mL | [72] | |
2000–2009 | Corn stover | Cellulases and hemicellulases | 1.2 Filter paper activity | FPU/mL | [11] |
Rice straw and wheat bran | Cellulases and hemicellulases | 129 CMCase 100 β-glucosidase 5070 Xylanase | IU/g | [73] | |
Sugar beet pulp | Endoglucanase, arabinosidase | 0.19 Endoglucanase 0.009 arabinosidase | U/mL | [74] | |
Sugar cane bagasse | Cellulases and xylanases | 0.13 FPA 0.33 Xylanases | U/mL | [75] | |
Wheat bran | Cellulolytic and hemicellulolytic enzymes | 1.05 endoglucanase 1.3 β-glucosidase 5.0 xylanase | U/mL | [76] | |
Wheat bran and sugar cane bagasse | Cellulases and xylanases | 32·89 FPA 10 Xylanase | U/g | [77] | |
Corn stover | Cellulolytic and xylanolytic enzymes | 304 endoglucanase 1840 Xylanases | U/g | [78] | |
Sorghum Bagasse | Cellulases and xylanases | 492.8 endoglucanase 297.8 Xylanases | U/g | [79] | |
Wheat straw | Cellulases | 3.2 FPA83 CMCase | IU/mL | [80] | |
Cassava waste | Cellulases | 0.46 CMCase 0.28 FPase | IU/mL | [81] | |
Wheat bran and rice straw | Cellulases | 62.5 endoglucanase 3.0 FPase 196 Xylanase | units/g substrate | [82] | |
2010–2020 | Horticulture waste | Cellulase and hemicellulase | 15 FPase 52.1 Xylanase | U/g | [83] |
Apple pomace | Cellulase and hemicellulase | 133.68 FPase 1412.58 Xylanase | IU/g | [84] | |
Agricultural wastes | Cellulase and xylanase | 13.57 Cellulase 3106.34 Xylanase | IU/g | [85] | |
Agricultural Wastes | Cellulase and xylanase | 30.22 FPase 427.0 Xylanase | U/g | [86] | |
Apple pomace | Cellulase and hemicellulase | 383.7 FPase 4868 Xylanase | IU/g | [87] | |
Sorghum and wheat bran | Cellulase and hemicellulase | 30.64 Cellulase 300.07 Xylanase | U/g | [88] | |
DDGS | Cellulase and hemicellulase | 0.592 Cellulase 34.8 Xylanase | IU/mL | [89] |
Type | Pretreatment Method | Microorganisms | Example of Pretreatment Method | Feedstock | Enzyme Production | References |
---|---|---|---|---|---|---|
Physical | Liquid hot water | Trichoderma reesei | 200 °C for 30 min | Corn Cob | 3.5 FPU/mL | [107] |
Steam | Trichoderma reesei | 121 °C for 2 h | Horticultural Waste | 72 U/g | [83] | |
Milling | Trichoderma reesei | Milled to 200 to 500 µm particle sizes | Horticultural Waste | 6.6 U/g | [83] | |
Microwave | Aspergillus heteromorphus | 22.5 min irradiation time at 30 g/L substrate concentration | Rice Straw and Hulls | 14.1 U/g | [108] | |
Chemical | Dilute acid hydrolysis | 11 different bacterial and fungal strains | 5% sulfuric acid at 120 °C for 30 mins with 20% solid load | Distillers’ Dried Grains with Solubles | 0.592 IU/mL | [89] |
Alkaline treatment | Endophytic Acremonium Species | 1% NaOH at 10% solid load | Sugarcane Bagasse | 0.14 U/mL | [101] | |
Biological | Fungal treatment | Piptoporus betulinus | 7 mm diameter mycelial discs | Rice Straw | 7.43 U/g | [109] |
- | Optimized Conditions | - | |||||
---|---|---|---|---|---|---|---|
Enzyme | pH | Temperature (°C) | Agitation (RPM) | Time (h) | Microorganism (s) | Increase in Production | References |
Cellulase | 4–4.5 | 28 | 120 | 96 | Aspergillus niger | 0.02 to 0.1813 IU/mL | [152] |
CMCase | 7.2 | 39.11 | 121 | NO | Bacillus subtilis | 0.43 to 0.56 U/mL | [138] |
Cellulase | 7.5 | 40 | NO | 96 | Different Pseudomonas and Bacillus species | 0.98–3.4 U/mL | [153] |
Cellulase | 4 | 35 | NO | 54 | Aspergillus niger | 0–0.37 IU/mL | [147] |
FPase | NO | 32.8 | NO | 144 | Trichoderma viride | 0.12 to 0.55 U/mL | [154] |
Xylanase | NO | 34.7 | NO | 158 | Trichoderma viride | 30 to 145 U/mL | [154] |
FPase | NO | 37 | NO | NO | Aspergillus fumigatus | 0–9.73 U/g | [155] |
CMCase | 5.5 | 30 | NO | 264 | Fomitopsis sp. | 0–71.7 IU/g | [156] |
CMCase | 5.5 | 50 | NO | NO | Paenibacillus terrae | 0.1–2.08 U/mL | [157] |
Xylanase | NO | NO | NO | 264 | Schizophyllum commune | 0.08–5,740 IU/mL | [158] |
Enzyme | Nitrogen Source Optimization | Microorganism (s) | Increase in Enzyme Activity | References |
---|---|---|---|---|
Cellulase | 0.125% peptone | Aspergillus niger | 0.05–0.1813 IU/mL | [152] |
Cellulase | 4 g/L NaNO3 | Penicillium occitanis | 0.5–13 U/mL | [159] |
FPase | 3% sulfite pulp | Trichoderma viride | 0.12–0.39 U/mL | [154] |
Xylanase | 3% sulfite pulp | Trichoderma viride | 30–70.25 U/mL | [154] |
FPase | 0.25% beef extract | Aspergillus fumigatus | 0–9.73 U/g | [155] |
FPase | 80.2 g/L Peptone | Sclerotium rolfsii | 0–5.72 FPU/mL | [141] |
Xylanase | 55.4 g/L yeast extract | Schizophyllum commune | 0.08–5.74 IU/mL | [158] |
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Iram, A.; Cekmecelioglu, D.; Demirci, A. Ideal Feedstock and Fermentation Process Improvements for the Production of Lignocellulolytic Enzymes. Processes 2021, 9, 38. https://doi.org/10.3390/pr9010038
Iram A, Cekmecelioglu D, Demirci A. Ideal Feedstock and Fermentation Process Improvements for the Production of Lignocellulolytic Enzymes. Processes. 2021; 9(1):38. https://doi.org/10.3390/pr9010038
Chicago/Turabian StyleIram, Attia, Deniz Cekmecelioglu, and Ali Demirci. 2021. "Ideal Feedstock and Fermentation Process Improvements for the Production of Lignocellulolytic Enzymes" Processes 9, no. 1: 38. https://doi.org/10.3390/pr9010038