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1.
Molecules ; 28(8)2023 Apr 18.
Artigo em Inglês | MEDLINE | ID: mdl-37110796

RESUMO

Coffee waste is often viewed as a problem, but it can be converted into value-added products if managed with clean technologies and long-term waste management strategies. Several compounds, including lipids, lignin, cellulose and hemicelluloses, tannins, antioxidants, caffeine, polyphenols, carotenoids, flavonoids, and biofuel can be extracted or produced through recycling, recovery, or energy valorization. In this review, we will discuss the potential uses of by-products generated from the waste derived from coffee production, including coffee leaves and flowers from cultivation; coffee pulps, husks, and silverskin from coffee processing; and spent coffee grounds (SCGs) from post-consumption. The full utilization of these coffee by-products can be achieved by establishing suitable infrastructure and building networks between scientists, business organizations, and policymakers, thus reducing the economic and environmental burdens of coffee processing in a sustainable manner.


Assuntos
Antioxidantes , Polifenóis , Lignina , Flavonoides , Cafeína , Resíduos/análise
2.
Molecules ; 25(18)2020 Sep 18.
Artigo em Inglês | MEDLINE | ID: mdl-32962056

RESUMO

In this research, novel biorefinery processes for obtaining value-added chemicals such as biosugar and hesperidin from mandarin peel waste (MPW) are described. Herein, three different treatment methods were comparatively evaluated to obtain high yields of biosugar and hesperidin from MPW. Each method was determined by changes in the order of three processing steps, i.e., oil removal, hesperidin extraction, and enzymatic hydrolysis. The order of the three steps was found to have a significant influence on the production yields. Biosugar and hesperidin production yields were highest with method II, where the processing steps were performed in the following order: oil removal, enzymatic hydrolysis, and hesperidin extraction. The maximum yields obtained with method II were 34.46 g of biosugar and 6.48 g of hesperidin per initial 100 g of dry MPW. Therefore, the methods shown herein are useful for the production of hesperidin and biosugar from MPW. Furthermore, the utilization of MPWs as sources of valuable materials may be of considerable economic benefits and has become increasingly attractive.


Assuntos
Citrus/metabolismo , Hesperidina/metabolismo , Açúcares/metabolismo , Biomassa , Celulases/metabolismo , Citrus/química , Frutas/química , Frutas/metabolismo , Hesperidina/química , Hesperidina/isolamento & purificação , Hidrólise , Extração Líquido-Líquido , Espectroscopia de Ressonância Magnética
3.
Bioresour Technol ; 395: 130363, 2024 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-38253244

RESUMO

Rice husk, rich carbon content, is an agricultural waste produced globally at an amount of 120 million tons annually, and it has high potential as a biorefinery feedstock. Herein, we investigated the feasibility of producing various products as D-psicose, bioethanol and lactic acid from rice husk (RH) through a biorefinery process. Alkali-hydrogen peroxide-acetic acid pretreatment of RH effectively removed lignin and silica, resulting in enzymatic hydrolysis yield of approximately 86.3% under optimal hydrolysis conditions. By using xylose isomerase as well as D-psicose-3-epimerase with borate, glucose present in the RH hydrolysate was converted into D-psicose with a 40.6% conversion yield in the presence of borate. Furthermore, bioethanol (85.4%) and lactic acid (92.5%) were successfully produced from the RH hydrolysate. This study confirmed the high potential of RH as a biorefinery feedstock, and it is expected that various platform chemicals and value-added products can be produced using RH.


Assuntos
Oryza , Oryza/química , Boratos , Ácido Láctico , Frutose , Hidrólise
4.
Bioresour Technol ; 372: 128694, 2023 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-36731613

RESUMO

Herein, we investigated the possibility of co-producing xylo-oligosaccharides (XOSs) from bamboo, as value-added products, along with succinic and lactic acids, as platform chemicals. Xylan was extracted from bamboo using the alkali method under mild conditions. From xylan, XOSs were produced by partial enzymatic hydrolysis at a conversion rate of 83.9%, and all reaction conditions resulted in similar degrees of polymerization. Hydrogen peroxide-acetic acid (HPAC) pretreatment effectively removed lignin from NaOH-treated bamboo, and the enzymatic hydrolytic yield of NaOH and HPAC-treated bamboo was 84.3% of the theoretical yield. The production of succinic and lactic acids from the hydrolysate resulted in conversion rates of approximately 63.2% and 91.3% of the theoretical yield using Corynebacterium glutamicum Δldh and Actinobacillus succinogenes, respectively, under facultative anaerobic conditions. This study demonstrates that bamboo has a high potential to produce value-added products using a biorefinery process and is an alternative resource for compounds typically derived from petroleum.


Assuntos
Ácido Láctico , Ácido Succínico , Fermentação , Ácido Succínico/química , Hidróxido de Sódio , Xilanos , Oligossacarídeos , Hidrólise , Peróxido de Hidrogênio
5.
Environ Sci Ecotechnol ; 15: 100238, 2023 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-36785801

RESUMO

The rate of textile waste generation worldwide has increased dramatically due to a rise in clothing consumption and production. Here, conversion of cotton-based, colored cotton-based, and blended cotton-polyethylene terephthalate (PET) textile waste materials into value-added chemicals (bioethanol, sorbitol, lactic acid, terephthalic acid (TPA), and ethylene glycol (EG)) via enzymatic hydrolysis and fermentation was investigated. In order to enhance the efficiency of enzymatic saccharification, effective pretreatment methods for each type of textile waste were developed, respectively. A high glucose yield of 99.1% was obtained from white cotton-based textile waste after NaOH pretreatment. Furthermore, the digestibility of the cellulose in colored cotton-based textile wastes was increased 1.38-1.75 times because of the removal of dye materials by HPAC-NaOH pretreatment. The blended cotton-PET samples showed good hydrolysis efficiency following PET removal via NaOH-ethanol pretreatment, with a glucose yield of 92.49%. The sugar content produced via enzymatic hydrolysis was then converted into key platform chemicals (bioethanol, sorbitol, and lactic acid) via fermentation or hydrogenation. The maximum ethanol yield was achieved with the white T-shirt sample (537 mL/kg substrate), which was 3.2, 2.1, and 2.6 times higher than those obtained with rice straw, pine wood, and oak wood, respectively. Glucose was selectively converted into sorbitol and LA at a yield of 70% and 83.67%, respectively. TPA and EG were produced from blended cotton-PET via NaOH-ethanol pretreatment. The integrated biorefinery process proposed here demonstrates significant potential for valorization of textile waste.

6.
J Plant Res ; 125(6): 793-804, 2012 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-22610130

RESUMO

Contrary to extensive researches on the roles of metallothioneins (MTs) in metal tolerance of animals, the roles of plant MTs in metal tolerance are largely under investigation. In this study, we evaluated the functional role of type 2 MT from Colocasia esculenta (CeMT2b) in Zn tolerance of tobacco and E. coli cells. Under Zn-stress conditions, transgenic tobacco overexpressing CeMT2b displayed much better seedling growth, a significant decrease in the levels of H(2)O(2) and an increase in Zn accumulation compared with the wild type. Overexpression of CeMT2b in E. coli greatly enhanced Zn tolerance and Zn accumulation under Zn stresses compared with control cells. CeMT2b bound 5.38 ± 0.29 atoms of Zn per protein. To identify a structural domain of CeMT2b for Zn binding, we investigated the growth of E. coli expressing each of the N-terminal, C-terminal, and central linker domains or a CNC motif deletion from the C-terminus of full-length CeMT2b. The results showed that the CNC motif is required for Zn tolerance, and the N-terminal domain is more effective in Zn tolerance than the C-terminal domain. Taken together, our results provide direct evidence for functional contributions of CeMT2b in Zn tolerance of tobacco and E. coli cells.


Assuntos
Colocasia/genética , Genes de Plantas , Metalotioneína/metabolismo , Nicotiana/efeitos dos fármacos , Zinco/farmacologia , Motivos de Aminoácidos , Clonagem Molecular , Meios de Cultura/metabolismo , Escherichia coli/genética , Escherichia coli/metabolismo , Vetores Genéticos/genética , Vetores Genéticos/metabolismo , Peróxido de Hidrogênio/metabolismo , Metalotioneína/genética , Dados de Sequência Molecular , Proteínas de Plantas/metabolismo , Raízes de Plantas/efeitos dos fármacos , Raízes de Plantas/crescimento & desenvolvimento , Plantas Geneticamente Modificadas/efeitos dos fármacos , Plantas Geneticamente Modificadas/genética , Plantas Geneticamente Modificadas/crescimento & desenvolvimento , Estrutura Terciária de Proteína , Espécies Reativas de Oxigênio/metabolismo , Plântula/genética , Plântula/crescimento & desenvolvimento , Alinhamento de Sequência , Nicotiana/genética , Nicotiana/crescimento & desenvolvimento , Zinco/metabolismo
7.
J Ind Microbiol Biotechnol ; 39(7): 1081-9, 2012 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-22395898

RESUMO

The endoglucanase (Cel5B) from the filamentous fungus Gloeophyllum trabeum was cloned and expressed without a signal peptide, and alanine residue 22 converted to glutamine in Pichia pastoris GS115. The DNA sequence of Cel5B had an open reading frame of 1,077 bp, encoding a protein of 359 amino acid residues with a molecular weight of 47 kDa. On the basis of sequence similarity, Cel5B displayed active site residues at Glu-175 and Glu-287. Both residues lost full hydrolytic activity when replaced with alanine through point mutation. The purified recombinant Cel5B showed very high specific activity, about 80- to 1,000-fold and 13- to 70-fold in comparison with other endoglucanases and cellobiohydrolase, on carboxymethylcellulose and filter paper, respectively, at pH 3.5 and 55°C. Cel5B displayed bifunctional characteristics under acidic conditions. The kinetic properties of the enzyme determined using a Lineweaver-Burk plot indicated that Cel5B is a catalytically efficient cellulolytic enzyme. These results suggest that Cel5B has high bifunctional endo- and exoglucanase activity under acidic conditions and is a good candidate for bioconversion of lignocellulose.


Assuntos
Basidiomycota/enzimologia , Basidiomycota/genética , Celulase/química , Celulase/metabolismo , Microbiologia Industrial , Sequência de Aminoácidos , Domínio Catalítico , Celulase/genética , Celulase/isolamento & purificação , Celulose 1,4-beta-Celobiosidase/genética , Celulose 1,4-beta-Celobiosidase/metabolismo , Clonagem Molecular , Escherichia coli/genética , Modelos Moleculares , Dados de Sequência Molecular , Pichia/genética , Alinhamento de Sequência
8.
Polymers (Basel) ; 14(1)2022 Jan 01.
Artigo em Inglês | MEDLINE | ID: mdl-35012188

RESUMO

Cellulase adsorption onto lignin decreases the productivity of enzymatic hydrolysis of lignocellulosic biomass. Here, adsorption of enzymes onto different types of lignin was investigated, and the five major enzymes-cellobiohydrolases (CBHs), endoglucanase (Cel7B), ß-glucosidase (Cel3A), xylanase (XYNIV), and mannanase (Man5A)-in a cellulase cocktail obtained from Trichoderma reesei were individually analyzed through SDS-PAGE and zymogram assay. Lignin was isolated from woody (oak and pine lignin) and herbaceous (rice straw and kenaf lignin) plants. The relative adsorption of CBHs compared to the control was in the range of 14.15-18.61%. The carbohydrate binding motif (CBM) of the CBHs contributed to higher adsorption levels in oak and kenaf lignin, compared to those in pine and rice lignin. The adsorption of endoglucanase (Cel7B) by herbaceous plant lignin was two times higher than that of woody lignin, whereas XYNIV showed the opposite pattern. ß-glucosidase (Cel3A) displayed the highest and lowest adsorption ratios on rice straw and kenaf lignin, respectively. Mannanase (Man5A) was found to have the lowest adsorption ratio on pine lignin. Our results showed that the hydrophobic properties of CBM and the enzyme structures are key factors in adsorption onto lignin, whereas the properties of specific lignin types indirectly affect adsorption.

9.
Biotechnol Biofuels ; 14(1): 37, 2021 Feb 06.
Artigo em Inglês | MEDLINE | ID: mdl-33549141

RESUMO

BACKGROUND: Woody plants with high glucose content are alternative bioresources for the production of biofuels and biochemicals. Various pretreatment methods may be used to reduce the effects of retardation factors such as lignin interference and cellulose structural recalcitrance on the degradation of the lignocellulose material of woody plants. RESULTS: A hydrogen peroxide-acetic acid (HPAC) pretreatment was used to reduce the lignin content of several types of woody plants, and the effect of the cellulose structural recalcitrance on the enzymatic hydrolysis was analyzed. The cellulose structural recalcitrance and the degradation patterns of the wood fibers in the xylem tissues of Quercus acutissima (hardwood) resulted in greater retardation in the enzymatic saccharification than those in the tracheids of Pinus densiflora (softwood). In addition to the HPAC pretreatment, the application of supplementary enzymes (7.5 FPU cellulase for 24 h) further increased the hydrolysis rate of P. densiflora from 61.42 to 91.94% whereas the same effect was not observed for Q. acutissima. It was also observed that endoxylanase synergism significantly affected the hydrolysis of P. densiflora. However, this synergistic effect was lower for other supplementary enzymes. The maximum concentration of the reducing sugars produced from 10% softwood was 89.17 g L-1 after 36 h of hydrolysis with 15 FPU cellulase and other supplementary enzymes. Approximately 80 mg mL-1 of reducing sugars was produced with the addition of 7.5 FPU cellulase and other supplementary enzymes after 36 h, achieving rapid saccharification. CONCLUSION: HPAC pretreatment removed the interference of lignin, reduced structural recalcitrance of cellulose in the P. densiflora, and enabled rapid saccharification of the woody plants including a high concentration of insoluble substrates with only low amounts of cellulase. HPAC pretreatment may be a viable alternative for the cost-efficient production of biofuels or biochemicals from softwood plant tissues.

10.
Bioresour Technol ; 298: 122386, 2020 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-31740245

RESUMO

Dwindling petroleum resources and increasing environmental concerns have stimulated the production of platform chemicals via biochemical processes through the use of renewable carbon sources. Various types of biomass wastes, which are biodegradable and vastly underutilized, are generated worldwide in huge quantities. They contain diverse chemical constituents, which may serve as starting points for the manufacture of a wide range of valuable bio-derived platform chemicals, intermediates, or end products via different conversion pathways. The valorization of inexpensive, abundantly available, and renewable biomass waste could provide significant benefits in response to increasing fossil fuel demands and manufacturing costs, as well as emerging environmental concerns. This review explores the potential for the use of available biomass waste to produce important chemicals, such as monosaccharides, oligosaccharides, biofuels, bioactive molecules, nanocellulose, and lignin, with a focus on commercially viable technologies.


Assuntos
Biocombustíveis , Lignina , Biomassa , Carbono
11.
Biomolecules ; 10(5)2020 05 23.
Artigo em Inglês | MEDLINE | ID: mdl-32456184

RESUMO

Here, we report an increase in biomass yield and saccharification in transgenic tobacco plants (Nicotiana tabacumL.) overexpressing thermostable ß-glucosidase from Thermotoga maritima, BglB, targeted to the chloroplasts and vacuoles. The transgenic tobacco plants showed phenotypic characteristics that were significantly different from those of the wild-type plants. The biomass yield and life cycle (from germination to flowering and harvest) of the transgenic tobacco plants overexpressing BglB were 52% higher and 36% shorter than those of the wild-type tobacco plants, respectively, indicating a change in the genome transcription levels in the transgenic tobacco plants. Saccharification in biomass samples from the transgenic tobacco plants was 92% higher than that in biomass samples from the wild-type tobacco plants. The transgenic tobacco plants required a total investment (US$/year) corresponding to 52.9% of that required for the wild-type tobacco plants, but the total biomass yield (kg/year) of the transgenic tobacco plants was 43% higher than that of the wild-type tobacco plants. This approach could be applied to other plants to increase biomass yields and overproduce ß-glucosidase for lignocellulose conversion.


Assuntos
Proteínas de Bactérias/genética , Biomassa , Nicotiana/genética , Plantas Geneticamente Modificadas/genética , beta-Glucosidase/genética , Proteínas de Bactérias/metabolismo , Plantas Geneticamente Modificadas/crescimento & desenvolvimento , Açúcares/metabolismo , Thermotoga maritima/genética , Termotolerância , Nicotiana/crescimento & desenvolvimento , Regulação para Cima , beta-Glucosidase/metabolismo
12.
Protein Expr Purif ; 65(2): 244-50, 2009 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-19116167

RESUMO

The chitinase producing Penicillium sp. LYG 0704 was procured from soil of the Chonnam National University crop field. The chitinase activity was detected after the first day which increased gradually and reached its maximum after 3 days of cultivation. The chitinase was purified from a culture medium by precipitation with isopropanol and column chromatography with Mono Q and Butyl-Sepharose. The molecular mass of chitinase was estimated to be 47 kDa by SDS-PAGE. Optimal pH and temperature were 5.0 and 40 degrees C, respectively. The N-terminal amino acid sequence of the enzyme was determined to be (1)AGSYRSVAYFVDWAI(15). The fully cloned gene, 1287 bp in size, encoded a single peptide of 429 amino acids. BLAST search of the chitinase gene sequence showed similarity with chitinase of Aspergillus fumigatus Af293 chitinase gene (58%) and A. fumigatus class V chitinase ChiB1 gene (56%).


Assuntos
Quitinases/isolamento & purificação , Quitinases/metabolismo , Penicillium/enzimologia , Proteínas Recombinantes de Fusão/isolamento & purificação , Proteínas Recombinantes de Fusão/metabolismo , 2-Propanol/química , Quitinases/química , Clonagem Molecular , Eletroforese em Gel de Poliacrilamida , Ativação Enzimática , Estabilidade Enzimática , Escherichia coli/genética , Escherichia coli/metabolismo , Concentração de Íons de Hidrogênio , Peso Molecular , Proteínas Recombinantes de Fusão/química , Temperatura
13.
Bioresour Technol ; 158: 239-47, 2014 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-24607460

RESUMO

The economical production of biofuels is hindered by the recalcitrance of lignocellulose to processing, causing high consumption of processing enzymes and impeding hydrolysis of pretreated lignocellulosic biomass. We determined the major rate-limiting factor in the hydrolysis of popping pre-treated rice straw (PPRS) by examining cellulase adsorption to lignin and cellulose, amorphogenesis of PPRS, and re-hydrolysis. Based on the results, equivalence between enzyme loading and the open structural area of cellulose was required to significantly increase productive adsorption of cellulase and to accelerate enzymatic saccharification of PPRS. Amorphogenesis of PPRS by phosphoric acid treatment to expand open structural area of the cellulose fibers resulted in twofold higher cellulase adsorption and increased the yield of the first re-hydrolysis step from 13% to 46%. The total yield from PPRS was increased to 84% after 3h. These results provide evidence that cellulose structure is one of major effects on the enzymatic hydrolysis.


Assuntos
Biocombustíveis , Metabolismo dos Carboidratos , Celulose/biossíntese , Adsorção , Reatores Biológicos , Eletroforese em Gel de Poliacrilamida , Hidrólise
14.
Enzyme Microb Technol ; 52(3): 170-6, 2013 Mar 05.
Artigo em Inglês | MEDLINE | ID: mdl-23410928

RESUMO

Endo-1,4-ß-xylanase A (XynA) from Schizophyllum commune was cloned into pPCZαA and expressed in Pichia pastoris GS115. The open reading frame of the xynA gene is composed of 684 bp, encoding 278 amino acids with a molecular weight of 26 kDa. Based on sequence similarity, XynA belongs to the CAZy glycoside hydrolase family 11. The optimal activity of XynA was at pH 5 and 50 °C on beechwood xylan. Under these conditions, the K(m), V(max) and specific activity of XynA were 5768 units mg(-1), 4 mg ml(-1) and 9000 µmol min(-1)mg(-1), respectively. XynA activity was enhanced in the presence of cations, such as K(+), Na(+), Li(2+), Cd(2+), and Co(2+). However, in the presence of EDTA, Hg(2+) and Fe(3+), xylanase activity was significantly inhibited. This enzyme effectively degraded approximately 45% of unsubstituted xylans in the cell wall from poplar stems. The high level of XynA activity might increase the yield of enzyme hydrolysis from biomass. Thus, XynA could be used as a major component of a lignocellulosic degrading enzyme cocktail.


Assuntos
Endo-1,4-beta-Xilanases/metabolismo , Proteínas Fúngicas/metabolismo , Pichia/metabolismo , Schizophyllum/enzimologia , Cátions/farmacologia , Quelantes/farmacologia , Clonagem Molecular , DNA Complementar/genética , Ácido Edético/farmacologia , Endo-1,4-beta-Xilanases/antagonistas & inibidores , Endo-1,4-beta-Xilanases/genética , Endo-1,4-beta-Xilanases/isolamento & purificação , Fagus , Proteínas Fúngicas/antagonistas & inibidores , Proteínas Fúngicas/genética , Proteínas Fúngicas/isolamento & purificação , Genes Fúngicos , Hidrólise , Imuno-Histoquímica , Cinética , Fases de Leitura Aberta , Populus , Proteínas Recombinantes de Fusão/metabolismo , Schizophyllum/genética , Análise de Sequência de DNA , Especificidade por Substrato , Madeira , Xilanos/metabolismo
15.
Chem Commun (Camb) ; 48(6): 886-8, 2012 Jan 21.
Artigo em Inglês | MEDLINE | ID: mdl-22139473

RESUMO

Three cystein-tagged cellulases co-immobilized on AuNP and Au-MSNP for the hydrolytic degradation of cellulose. The biochemical properties, stabilities, activities and reusability of these co-immobilized systems were compared to those of mixtures of free cellulases.


Assuntos
Celulases/química , Celulose/química , Enzimas Imobilizadas/química , Ouro/química , Nanopartículas Metálicas/química , Dióxido de Silício/química , Temperatura Alta , Concentração de Íons de Hidrogênio , Magnetismo , Nanopartículas Metálicas/ultraestrutura , Microscopia Eletrônica de Varredura , Microscopia Eletrônica de Transmissão
16.
Mol Biotechnol ; 49(3): 229-39, 2011 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-21424337

RESUMO

A gene (arf) encoding an α-L: -arabinofuranosidase (ARF) that hydrolyzes arabinose substituted on xylan was isolated from Penicillium sp. The gene was predicted to encode 339 amino acid residues showing 71-75% homology to GH family 54. E. coli expressed ARF showed optimal activity at 50°C and pH 5-6 on wheat arabinoxylan. The hydrolysis activities on oat spelt xylan by ARF and xylanase were 1.67-fold higher than that of xylanase alone. The synergistic effects of ARF and commercial enzymes (xylanase and cellulase) on popping-pretreated rice straw were 1.15-1.51-fold higher amounts of sugars released in the [ARF + xylanase + cellulase] mixture than in the mixtures [ARF + xylanase], [ARF + cellulase], and [xylanase + cellulase]. Moreover, the liberation of arabinose by ARF was enhanced 2.1-2.9-fold in a reaction with xylanase and cellulase as compared with [xylanase + cellulase] and ARF alone.


Assuntos
Glicosídeo Hidrolases/genética , Lignina/metabolismo , Penicillium/enzimologia , Sequência de Aminoácidos , Arabinose/análise , Avena/metabolismo , Sequência de Bases , Domínio Catalítico , Clonagem Molecular , Endo-1,4-beta-Xilanases/metabolismo , Genes Fúngicos/genética , Glucose/análise , Glicosídeo Hidrolases/química , Hidrólise , Dados de Sequência Molecular , Oryza/metabolismo , Penicillium/genética , Alinhamento de Sequência , Resíduos , Xilanos/metabolismo , Xilanos/ultraestrutura , Xilose/análise
17.
Bioresour Technol ; 102(10): 5788-93, 2011 May.
Artigo em Inglês | MEDLINE | ID: mdl-21376577

RESUMO

The objective of this study was to find a pretreatment process that enhances enzymatic conversion of biomass to sugars. Rapeseed straw was pretreated by two processes: a wet process involving wet milling plus a popping treatment, and a dry process involving popping plus dry milling. The effects of the pretreatments were studied both in terms of structural and compositional changes and change in susceptibility to enzymatic hydrolysis. After application of the wet and dry processes, the amounts of cellulose and xylose in the straw were 37-38% and 14-15%, respectively, compared to 31% and 12% in untreated counterparts. In enzymatic hydrolysis performance, the wet process presented the best glucose yield, with a 93.1% conversion, while the dry process yielded 69.6%, and the un-pretreated process yielded <20%. Electron microscopic studies of the straw also showed a relative increase in susceptibility to enzymatic hydrolysis with pretreatment.


Assuntos
Brassica rapa/metabolismo , Enzimas/metabolismo , Etanol/metabolismo , Celulose/metabolismo , Hidrólise , Propriedades de Superfície , Difração de Raios X , Xilose/metabolismo
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