Combined use of mild oxidation and cutinase/lipase pretreatments for enzymatic processing of wool fabrics

Wang, Ping; Cui, Li; Wang, Qiang; Fan, Xuerong; Zhao, Xia; Wu, Jing

doi:10.1002/elsc.200900041

Cited by 18 publications

(7 citation statements)

References 16 publications

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“…Wang et al (2010) showed results of cutinase applications in enzymatic processes of pretreating the tissue. The authors showed that cutinases act as modifier agents of the polymer surface, by facilitating the absorption of other substances in different treatments.…”

Section: Application Of Cut and Cut-n1 In The Degradation Of Plasticsmentioning

confidence: 99%

Production of heterologous cutinases by E. coli and improved enzyme formulation for application on plastic degradation

Gomes¹,

Matamá²,

Cavaco‐Paulo³

et al. 2013

Electron. J. Biotechnol.

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Background: The hydrolytic action of cutinases has been applied to the degradation of plastics. Polyethylene terephthalate (PET) have long half-life which constitutes a major problem for their treatment as urban solid residues. The aim of this work was to characterize and to improve stable the enzyme to optimize the process of degradation using enzymatic hydrolysis of PET by recombinant cutinases. Results:The wild type form of cutinase from Fusarium solani pisi and its C-terminal fusion to cellulose binding domain N1 from Cellulomonas fimi were produced by genetically modified Escherichia coli. The maximum activity of cutinases produced in Lactose Broth in the presence of ampicillin and isopropyl β-D-1-thiogalactopyranoside (IPTG) was 1.4 IU/mL. Both cutinases had an optimum pH around 7.0 and they were stable between 30 and 50ºC during 90 min. The addition of glycerol, PEG-200 and (NH4)2SO4 to the metabolic liquid, concentrated by ultra filtration, stabilized the activity during 60 days at 28ºC. The treatment of PET with cutinases during 48 hrs led to maxima weight loss of 0.90%. Conclusions: Recombinant microbial cutinases may present advantages in the treatment of poly(ethylene terephthalate) PET through enzymatic treatments.

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Section: Application Of Cut and Cut-n1 In The Degradation Of Plasticsmentioning

confidence: 99%

Production of heterologous cutinases by E. coli and improved enzyme formulation for application on plastic degradation

Gomes¹,

Matamá²,

Cavaco‐Paulo³

et al. 2013

Electron. J. Biotechnol.

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“…Wang et al . used a mild oxidation and cutinase/lipase pretreatment process and the area shrinkage of worsted wool fabric decreased to 3.1% 19. In Cortez et al study, after permonossulphuric acid pretreatment, the knitted wool fabric was then treated with either tissue or microbial TGase from S. mobaraense and the area shrinkage level was reduced from 16 to 6% 20.…”

Section: Resultsmentioning

confidence: 99%

Casein and transglutaminase‐mediated modification of wool surface

Cui

Fan

Wang

et al. 2011

Engineering in Life Sciences

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In this study, casein, a protein found in milk, was used as a surface‐coating material for improving wool fabric properties mediated by a microbial protein cross‐linking enzyme: transglutaminase (TGase). For the wool fabric used in this study, 4% casein (owf) treatment for 1 h combined with 20 U/g fabric of microbial TGase reduced the area shrinkage of the KMnO4‐pretreated wool fabric from 11.32±0.26 to 4.57±0.15%. The tensile strength increased from 275±5.0 to 315±2.1 N. The casein cross‐linked by TGase on wool exhibited better stability than that with the inactivated enzyme in warm water, Na2CO3 and SDS solutions. Scanning electron micrographs demonstrated that the casein and TGase treatment smoothened the wool fiber surface by coating or filling the raised scales of the wool.

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“…There are many reports on application of enzymes on different textile goods [4][5][6][7][8][9][10][11].…”

Section: Introductionmentioning

confidence: 99%

Treatment of Bleached Wool with Trans-Glutaminases to Enhance Tensile Strength, Whiteness, and Alkali Resistance

Montazer

Lessan

Pajootan

et al. 2011

Appl Biochem Biotechnol

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Trans-glutaminases is known as a cross-linking enzyme for proteins. Wool is a proteinous fiber conventionally is treated through several processes to obtain the desirable characteristics. Bleaching is also one of the most important processes usually carried out by using an oxidizing agent in a conventional method. The tensile strength of wool yarns was reduced as a consequence of oxidative bleaching. Here, with the help of microbial trans-glutaminases (m-TGases), a novel bleaching process was disclosed in a way to obtain a bleached wool yarn with no significant reduction in the tensile strength. The results confirmed that the bleached wool yarns with H(2)O(2) could be modified by m-TGases post-treatment. The m-TGases treatment on the bleached wool yarns improved the tensile strength and whiteness along with the higher alkali resistance.

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Combined use of mild oxidation and cutinase/lipase pretreatments for enzymatic processing of wool fabrics

Cited by 18 publications

References 16 publications

Production of heterologous cutinases by E. coli and improved enzyme formulation for application on plastic degradation

Production of heterologous cutinases by E. coli and improved enzyme formulation for application on plastic degradation

Casein and transglutaminase‐mediated modification of wool surface

Treatment of Bleached Wool with Trans-Glutaminases to Enhance Tensile Strength, Whiteness, and Alkali Resistance

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