Enzyme processing of textiles in reverse micellar solution

Sawada, Kazuya; Ueda, Mitsuo

doi:10.1016/s0168-1656(01)00310-8

Cited by 52 publications

(34 citation statements)

References 7 publications

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“…21 From these results, the activity of enzymes in the Tween-85 reverse micellar system seems to follow Michaelis-Menten kinetics. As reported previously, 17 the enzyme in an anionic surfactant reverse micellar system showed peculiar activity due to an influence of ionic head groups of surfactant molecules. Applications of non-ionic surfactant which can overcome an influence of the charge would reduce adverse effects on the activity of the enzyme.…”

Section: Resultssupporting

confidence: 73%

“…In fact, our previous study indicated that the activity of some enzymes solubilized in anionic surfactant reverse micellar systems was markedly different from that in aqueous systems. 17 At this time the unusual activity of enzymes in anionic surfactant reverse micellar systems cannot easily be explained, but it may be related to the uneven polar environment of the water-pool. In addition, the lower dielectric constant in the water-pool, enzyme-surfactant interactions, conformational changes of enzymes, etc may also be taken into account.…”

Section: Introductionmentioning

confidence: 99%

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Characteristics of aqueous microenvironments in non‐ionic surfactant reverse micelles and their use for enzyme reactions in non‐aqueous media

Sawada

Ueda

2004

J of Chemical Tech & Biotech

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The polarity of water solubilized in the interior of non-ionic surfactant reverse micellar systems has been investigated using optical probes. Small amounts of water incorporated on the inside of various reverse micellar systems, polyoxyethylene sorbitan trioleate (Tween-85)/isopropyl alcohol/nhexane mixture and polyoxyethylene tert-octylphenyl ether (TX-100)/cyclohexane, were found to have low polarity compared with bulk water. The polarity of water in both Tween-85 and TX-100 reverse micellar systems corresponded to that of methanol. The activity of the proteases α-chymotrypsin and subtilisin in Tween-85 and TX-100 reverse micellar systems has also been investigated. It was found that the amounts of water in the reverse micellar system have a significant influence on the activity of enzymes. In the TX-100 reverse micellar system, neither enzymes showed any activity. In contrast, the activity of enzymes in the Tween-85 reverse micellar system was similar to that in the aqueous system and followed standard Michaelis-Menten kinetics.

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Section: Resultssupporting

confidence: 73%

Section: Introductionmentioning

confidence: 99%

Characteristics of aqueous microenvironments in non‐ionic surfactant reverse micelles and their use for enzyme reactions in non‐aqueous media

Sawada

Ueda

2004

J of Chemical Tech & Biotech

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“…During the process of scouring in the textile industry, the cuticle layer has to be removed in order to improve the wettability of cotton fiber, which then facilitates uniform dyeing and finishing. Traditionally, this process is performed by hot hydrolysis in alkaline medium, which not only consumes large quantities of water and energy but also causes severe pollution and fiber damage (20,21,33). Therefore, environment-friendly scouring methods based on biocatalysts have been actively sought (2,30,36).…”

mentioning

confidence: 99%

Characterization of Thermobifida fusca Cutinase-Carbohydrate-Binding Module Fusion Proteins and Their Potential Application in Bioscouring

Zhang

Chen

et al. 2010

Appl Environ Microbiol

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Cutinase from Thermobifida fusca is thermally stable and has potential application in the bioscouring of cotton in the textile industry. In the present study, the carbohydrate-binding modules (CBMs) from T. fusca cellulase Cel6A (CBM Cel6A ) and Cellulomonas fimi cellulase CenA (CBM CenA ) were fused, separately, to the carboxyl terminus of T. fusca cutinase. Both fusion enzymes, cutinase-CBM Cel6A and cutinase-CBM CenA , were expressed in Escherichia coli and purified to homogeneity. Enzyme characterization showed that both displayed similar catalytic properties and pH stabilities in response to T. fusca cutinase. In addition, both fusion proteins displayed an activity half-life of 53 h at their optimal temperature of 50°C. Compared to T. fusca cutinase, in the absence of pectinase, the binding activity on cotton fiber was enhanced by 2% for cutinase-CBM Cel6A and by 28% for cutinase-CBM CenA , whereas in the presence of pectinase, the binding activity was enhanced by 40% for the former and 45% for the latter. Notably, a dramatic increase of up to 3-fold was observed in the amount of released fatty acids from cotton fiber by both cutinase-CBM fusion proteins when acting in concert with pectinase. This is the first report of improving the scouring efficiency of cutinase by fusing it with CBM. The improvement in activity and the strong synergistic effect between the fusion proteins and pectinase suggest that they may have better applications in textile bioscouring than the native cutinase.Cotton fiber has a multilayered structure, with its outermost surface being the cuticle that is cross-linked to the primary cell wall of cotton fiber by esterified pectin substances. The major component of the cuticle is cutin, an insoluble polyester composed mainly of saturated C 16 and C 18 hydroxy and epoxy fatty acids (14,16,27,38). During the process of scouring in the textile industry, the cuticle layer has to be removed in order to improve the wettability of cotton fiber, which then facilitates uniform dyeing and finishing. Traditionally, this process is performed by hot hydrolysis in alkaline medium, which not only consumes large quantities of water and energy but also causes severe pollution and fiber damage (20,21,33). Therefore, environment-friendly scouring methods based on biocatalysts have been actively sought (2,30,36).Cutinase is a multifunctional esterase capable of degrading the cutin component of the cuticle. Earlier reports showed that the fungal cutinase from Fusarium solani pisi has potential use for cotton cuticle degradation and exhibits a good synergistic effect with pectinase, an enzyme utilized to degrade pectin, in the scouring of cotton fiber (1,7,8,14). Moreover, site-directed mutagenesis has been performed to replace the specific amino acid residues near the active site of cutinase (3) to improve its hydrolytic activity toward polyesters. More recently, a cutinase from the thermophilic bacterium Thermobifida fusca has been identified and overexpressed in Escherichia coli in our laboratory (10). The...

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“…A degomagem de fibras de rami com pectina liase produz fibras com qualidade superior àquelas produzidas por complexos enzimáticos comerciais ou utilizando processo químico com soda alcalina, além de reduzir a poluição ambiental provocada pela liberação da soda cáustica 28,46 . Em algodão cru, a remoção da pectina, cera e agentes de goma com a utilização de pectinases em conjunto com amilases, lipases e hemicelulases em condições adequadas, substitui o uso da soda cáus-tica e gera produtos de alta qualidade, para posterior tingimento e processo de tecelagem com menor consumo de energia 47 .…”

Section: Indústria Têxtilunclassified

Pectinases: aplicações industriais e perspectivas

Uenojo¹,

Pastore²

2007

Quím. Nova

105

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Recebido em 15/8/05; aceito em 16/5/06; publicado na web em 19/1/07 PECTINOLYTIC ENZYMES. INDUSTRIAL APPLICATIONS AND FUTURE PERSPECTIVES. Pectic substances are structural heteropolysaccharides that occur in the middle lamellae and primary cell walls of higher plants. They are composed of partially methylesterified galacturonic acid residues linked by α-1, 4-glycosidic bonds. Pectinolytic enzymes are complex enzymes that degrade pectic polymers and there are several classes of enzymes, which include pectin esterases, pectin and pectate lyases and polygalacturonases. Plants, filamentous fungi, bacteria and yeasts are able to produce pectinases. In the industrial world, pectinases are used in fruit juice clarification, in the production of wine, in the extraction of olive oil, fiber degumming and fermentation of tea, coffee and cocoa.

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Enzyme processing of textiles in reverse micellar solution

Cited by 52 publications

References 7 publications

Characteristics of aqueous microenvironments in non‐ionic surfactant reverse micelles and their use for enzyme reactions in non‐aqueous media

Characteristics of aqueous microenvironments in non‐ionic surfactant reverse micelles and their use for enzyme reactions in non‐aqueous media

Characterization of Thermobifida fusca Cutinase-Carbohydrate-Binding Module Fusion Proteins and Their Potential Application in Bioscouring

Pectinases: aplicações industriais e perspectivas

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