Artur Cavaco-Paulo - Academia.edu (original) (raw)

Uploads

Papers by Artur Cavaco-Paulo

Research paper thumbnail of MALDI-TOF Mass Spectrometry in Textile Industry

NATO Science for Peace and Security Series A: Chemistry and Biology, 2008

Research paper thumbnail of Characterization of ligno-cellulosic materials bleached with oxo-diperoxo-molybdates

Carbohydrate Polymers, 2013

Research paper thumbnail of REVIEW ARTICLE - Protein interactions in enzymatic processes in textiles

Research paper thumbnail of Straighten curly hair with keratin peptides

Research paper thumbnail of Insights on the mechanical behavior of keratin fibrils

International Journal of Biological Macromolecules, Aug 1, 2016

Research paper thumbnail of Assessment of liposome disruption to quantify drug delivery in vitro

Biochimica Et Biophysica Acta - Biomembranes, Feb 1, 2016

Research paper thumbnail of The effects of solvent composition on the affinity of a peptide towards hair keratin: experimental and molecular dynamics data

Research paper thumbnail of Understanding the molecular basis behind hair morphology: development of new strategies to modulate hair from the follicle

Research paper thumbnail of Antimicrobial coating of textiles by laccase in situ polymerization of catechol and p-phenylenediamine

Reactive and Functional Polymers, 2018

Research paper thumbnail of Bio-coloration of bacterial cellulose assisted by immobilized laccase

AMB Express, Jan 13, 2018

In this work a process for the bio-coloration of bacterial cellulose (BC) membranes was developed... more In this work a process for the bio-coloration of bacterial cellulose (BC) membranes was developed. Laccase from Myceliophthora thermophila was immobilized onto BC membranes and retained up to 88% of residual activity after immobilization. Four compounds belonging to the flavonoids family were chosen to test the in situ polymerase activity of immobilized laccase. All the flavonoids were successfully polymerized by laccase giving rise to yellow, orange and dark brown oligomers which conferred color to the BC support. The optimal bio-coloration conditions were studied for two of the tested flavonoids, catechol and catechin, by varying the concentration and time of incubation. High color depth and resistance to washing were obtained for both compounds. The highly porous bacterial cellulose material demonstrated great performance as a bio-coloration support, in contrast to other materials cited in literature, like cotton or wool. The process developed is presented as an environmentally f...

Research paper thumbnail of Practical insights on enzyme stabilization

Critical reviews in biotechnology, 2017

Enzymes are efficient catalysts designed by nature to work in physiological environments of livin... more Enzymes are efficient catalysts designed by nature to work in physiological environments of living systems. The best operational conditions to access and convert substrates at the industrial level are different from nature and normally extreme. Strategies to isolate enzymes from extremophiles can redefine new operational conditions, however not always solving all industrial requirements. The stability of enzymes is therefore a key issue on the implementation of the catalysts in industrial processes which require the use of extreme environments that can undergo enzyme instability. Strategies for enzyme stabilization have been exhaustively reviewed, however they lack a practical approach. This review intends to compile and describe the most used approaches for enzyme stabilization highlighting case studies in a practical point of view.

Research paper thumbnail of Effect of a peptide in cosmetic formulations for hair volume control

International journal of cosmetic science, Jan 13, 2017

The capacity of hair to absorb water causes changes in its physical and cosmetic properties under... more The capacity of hair to absorb water causes changes in its physical and cosmetic properties under different environmental conditions. Hence, the control of hair volume in variable relative humidity settings is an important topic in cosmetics. The behaviour of two types of hair, Caucasian and Asian, was studied regarding their volume change in different relative humidity conditions. The ability of a peptide as a hair volume treatment was evaluated in two climate control formulations. Tresses of the two types of hair were tested in two relative humidity (RH) conditions: (A) variable relative humidity (2 hours 40% RH, followed by 2 hours 90% RH and 2 hours of 40% RH), and (B) continuous high relative humidity (90% RH for 6 hours). Changes in the hair tress volume were assessed throughout time. Hair treated with two climate control formulations, with and without a peptide (KP peptide), were tested under the two relative humidity conditions. Caucasian hair had a higher change in volume c...

Research paper thumbnail of Peptide—protein interactions within human hair keratins

International Journal of Biological Macromolecules, 2017

Research paper thumbnail of Enzymatic Treatments to Improve Mechanical Properties and Surface Hydrophobicity of Jute Fiber Membranes

Research paper thumbnail of Human Hair and the Impact of Cosmetic Procedures: A Review on Cleansing and Shape-Modulating Cosmetics

Research paper thumbnail of Enzymatic phosphorylation of hair keratin enhances fast adsorption of cationic moieties

International Journal of Biological Macromolecules, 2016

Research paper thumbnail of Cutinase promotes dry esterification of cotton cellulose

Biotechnology progress, Jan 12, 2015

Cutinase from Thermobifida fusca was used to esterify the hydroxyl groups of cellulose with the f... more Cutinase from Thermobifida fusca was used to esterify the hydroxyl groups of cellulose with the fatty acids from triolein. Cutinase and triolein were pre-adsorbed on cotton and the reaction proceeded in a dry state during 48 hours at 35ºC. The cutinase-catalyzed esterification of the surface of cotton fabric resulted in the linkage of the oleate groups to the glycoside units of cotton cellulose. The superficial modification was confirmed by performing ATR-FTIR on treated cotton samples and by MALDI-TOF analysis of the liquors from the treatment of the esterified cotton with a crude cellulase mixture. Modified cotton fabric also showed a significant increase of hydrophobicity. This work proposes a novel bio-based approach to obtain hydrophobic cotton. This article is protected by copyright. All rights reserved.

Research paper thumbnail of Enzymatic processing of protein-based fibers

Applied microbiology and biotechnology, 2015

Wool and silk are major protein fiber materials used by the textile industry. Fiber protein struc... more Wool and silk are major protein fiber materials used by the textile industry. Fiber protein structure-function relationships are briefly described here, and the major enzymatic processing routes for textiles and other novel applications are deeply reviewed. Fiber biomodification is described here with various classes of enzymes such as protease, transglutaminase, tyrosinase, and laccase. It is expected that the reader will get a perspective on the research done as a basis for new applications in other areas such as cosmetics and pharma.

Research paper thumbnail of Laccase Polymerization of Amino-Phenol Compounds

Laccases are a multi-copper phenol oxidase, which reduces oxygen to water and simultaneously cata... more Laccases are a multi-copper phenol oxidase, which reduces oxygen to water and simultaneously catalyze the oxidation of aromatic pollutant such anilines and phenols [1, 2]. Several methods using laccase, immobilized laccase and laccase/mediator system have been developed for the treatment of the textile effluents [3-11]. This enzyme decolorizes some azo dyes without direct cleavage of the azo bond through a highly non-specific free radical mechanism, thereby avoiding the formation of toxic aromatic amines [12]. However, the substrate specificity of laccase limits the number of azo dyes that can be degraded [13]. Another possibility is the use of an azo reductase bacteria, that under microaerophilic condition can cleave a wider range of azo dyes into corresponding toxics aromatic amine [12, 14, 15], associated with a laccase [16].The microaerophilic condition has permitted the simultaneously presence, in the medium, of the azo reductase and a Trametes villosa laccase that is able to p...

Research paper thumbnail of Sono-Enzymatic Polymerization of Catechol

The potential of laccase enzymes for polymerizing, crosslinking and functionalizing various compo... more The potential of laccase enzymes for polymerizing, crosslinking and functionalizing various compounds was studied extensively and increasing interest has been focused on the application of this enzyme as a new biocatalyst in organic synthesis.[1-6] Laccases (EC 1.10.3.2) are a class of multi-copper-containing oxidoreductase enzymes able to catalyze the transformation of various aromatic compounds, specifically phenols and anilines, through the formation of a free cation radical after the transfer of a single electron to laccase. The radical can further react on non-enzymatic oxidation polymerizing various halogen, alkyl-, alkoxy-substituted anilines and phenols.[7-8] The phenolic derivatives resulting in the production of polymeric aggregates are usually less soluble and much stable than their parent compounds.[9,10] Unfortunately the relatively short catalytic lifetime of the laccases in the polymerization processes and the mass transfer limitations, restrict their applications. Th...

Research paper thumbnail of MALDI-TOF Mass Spectrometry in Textile Industry

NATO Science for Peace and Security Series A: Chemistry and Biology, 2008

Research paper thumbnail of Characterization of ligno-cellulosic materials bleached with oxo-diperoxo-molybdates

Carbohydrate Polymers, 2013

Research paper thumbnail of REVIEW ARTICLE - Protein interactions in enzymatic processes in textiles

Research paper thumbnail of Straighten curly hair with keratin peptides

Research paper thumbnail of Insights on the mechanical behavior of keratin fibrils

International Journal of Biological Macromolecules, Aug 1, 2016

Research paper thumbnail of Assessment of liposome disruption to quantify drug delivery in vitro

Biochimica Et Biophysica Acta - Biomembranes, Feb 1, 2016

Research paper thumbnail of The effects of solvent composition on the affinity of a peptide towards hair keratin: experimental and molecular dynamics data

Research paper thumbnail of Understanding the molecular basis behind hair morphology: development of new strategies to modulate hair from the follicle

Research paper thumbnail of Antimicrobial coating of textiles by laccase in situ polymerization of catechol and p-phenylenediamine

Reactive and Functional Polymers, 2018

Research paper thumbnail of Bio-coloration of bacterial cellulose assisted by immobilized laccase

AMB Express, Jan 13, 2018

In this work a process for the bio-coloration of bacterial cellulose (BC) membranes was developed... more In this work a process for the bio-coloration of bacterial cellulose (BC) membranes was developed. Laccase from Myceliophthora thermophila was immobilized onto BC membranes and retained up to 88% of residual activity after immobilization. Four compounds belonging to the flavonoids family were chosen to test the in situ polymerase activity of immobilized laccase. All the flavonoids were successfully polymerized by laccase giving rise to yellow, orange and dark brown oligomers which conferred color to the BC support. The optimal bio-coloration conditions were studied for two of the tested flavonoids, catechol and catechin, by varying the concentration and time of incubation. High color depth and resistance to washing were obtained for both compounds. The highly porous bacterial cellulose material demonstrated great performance as a bio-coloration support, in contrast to other materials cited in literature, like cotton or wool. The process developed is presented as an environmentally f...

Research paper thumbnail of Practical insights on enzyme stabilization

Critical reviews in biotechnology, 2017

Enzymes are efficient catalysts designed by nature to work in physiological environments of livin... more Enzymes are efficient catalysts designed by nature to work in physiological environments of living systems. The best operational conditions to access and convert substrates at the industrial level are different from nature and normally extreme. Strategies to isolate enzymes from extremophiles can redefine new operational conditions, however not always solving all industrial requirements. The stability of enzymes is therefore a key issue on the implementation of the catalysts in industrial processes which require the use of extreme environments that can undergo enzyme instability. Strategies for enzyme stabilization have been exhaustively reviewed, however they lack a practical approach. This review intends to compile and describe the most used approaches for enzyme stabilization highlighting case studies in a practical point of view.

Research paper thumbnail of Effect of a peptide in cosmetic formulations for hair volume control

International journal of cosmetic science, Jan 13, 2017

The capacity of hair to absorb water causes changes in its physical and cosmetic properties under... more The capacity of hair to absorb water causes changes in its physical and cosmetic properties under different environmental conditions. Hence, the control of hair volume in variable relative humidity settings is an important topic in cosmetics. The behaviour of two types of hair, Caucasian and Asian, was studied regarding their volume change in different relative humidity conditions. The ability of a peptide as a hair volume treatment was evaluated in two climate control formulations. Tresses of the two types of hair were tested in two relative humidity (RH) conditions: (A) variable relative humidity (2 hours 40% RH, followed by 2 hours 90% RH and 2 hours of 40% RH), and (B) continuous high relative humidity (90% RH for 6 hours). Changes in the hair tress volume were assessed throughout time. Hair treated with two climate control formulations, with and without a peptide (KP peptide), were tested under the two relative humidity conditions. Caucasian hair had a higher change in volume c...

Research paper thumbnail of Peptide—protein interactions within human hair keratins

International Journal of Biological Macromolecules, 2017

Research paper thumbnail of Enzymatic Treatments to Improve Mechanical Properties and Surface Hydrophobicity of Jute Fiber Membranes

Research paper thumbnail of Human Hair and the Impact of Cosmetic Procedures: A Review on Cleansing and Shape-Modulating Cosmetics

Research paper thumbnail of Enzymatic phosphorylation of hair keratin enhances fast adsorption of cationic moieties

International Journal of Biological Macromolecules, 2016

Research paper thumbnail of Cutinase promotes dry esterification of cotton cellulose

Biotechnology progress, Jan 12, 2015

Cutinase from Thermobifida fusca was used to esterify the hydroxyl groups of cellulose with the f... more Cutinase from Thermobifida fusca was used to esterify the hydroxyl groups of cellulose with the fatty acids from triolein. Cutinase and triolein were pre-adsorbed on cotton and the reaction proceeded in a dry state during 48 hours at 35ºC. The cutinase-catalyzed esterification of the surface of cotton fabric resulted in the linkage of the oleate groups to the glycoside units of cotton cellulose. The superficial modification was confirmed by performing ATR-FTIR on treated cotton samples and by MALDI-TOF analysis of the liquors from the treatment of the esterified cotton with a crude cellulase mixture. Modified cotton fabric also showed a significant increase of hydrophobicity. This work proposes a novel bio-based approach to obtain hydrophobic cotton. This article is protected by copyright. All rights reserved.

Research paper thumbnail of Enzymatic processing of protein-based fibers

Applied microbiology and biotechnology, 2015

Wool and silk are major protein fiber materials used by the textile industry. Fiber protein struc... more Wool and silk are major protein fiber materials used by the textile industry. Fiber protein structure-function relationships are briefly described here, and the major enzymatic processing routes for textiles and other novel applications are deeply reviewed. Fiber biomodification is described here with various classes of enzymes such as protease, transglutaminase, tyrosinase, and laccase. It is expected that the reader will get a perspective on the research done as a basis for new applications in other areas such as cosmetics and pharma.

Research paper thumbnail of Laccase Polymerization of Amino-Phenol Compounds

Laccases are a multi-copper phenol oxidase, which reduces oxygen to water and simultaneously cata... more Laccases are a multi-copper phenol oxidase, which reduces oxygen to water and simultaneously catalyze the oxidation of aromatic pollutant such anilines and phenols [1, 2]. Several methods using laccase, immobilized laccase and laccase/mediator system have been developed for the treatment of the textile effluents [3-11]. This enzyme decolorizes some azo dyes without direct cleavage of the azo bond through a highly non-specific free radical mechanism, thereby avoiding the formation of toxic aromatic amines [12]. However, the substrate specificity of laccase limits the number of azo dyes that can be degraded [13]. Another possibility is the use of an azo reductase bacteria, that under microaerophilic condition can cleave a wider range of azo dyes into corresponding toxics aromatic amine [12, 14, 15], associated with a laccase [16].The microaerophilic condition has permitted the simultaneously presence, in the medium, of the azo reductase and a Trametes villosa laccase that is able to p...

Research paper thumbnail of Sono-Enzymatic Polymerization of Catechol

The potential of laccase enzymes for polymerizing, crosslinking and functionalizing various compo... more The potential of laccase enzymes for polymerizing, crosslinking and functionalizing various compounds was studied extensively and increasing interest has been focused on the application of this enzyme as a new biocatalyst in organic synthesis.[1-6] Laccases (EC 1.10.3.2) are a class of multi-copper-containing oxidoreductase enzymes able to catalyze the transformation of various aromatic compounds, specifically phenols and anilines, through the formation of a free cation radical after the transfer of a single electron to laccase. The radical can further react on non-enzymatic oxidation polymerizing various halogen, alkyl-, alkoxy-substituted anilines and phenols.[7-8] The phenolic derivatives resulting in the production of polymeric aggregates are usually less soluble and much stable than their parent compounds.[9,10] Unfortunately the relatively short catalytic lifetime of the laccases in the polymerization processes and the mass transfer limitations, restrict their applications. Th...