Surface Chemical Analysis of Lipase Enzyme Treatments on Wool and Mohair

Mall, J. K.; Sims, Paul F. G.; Carr, C.

doi:10.1080/00405000208630551

Cited by 16 publications

(3 citation statements)

References 16 publications

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“…26 Other researchers have used TOF-SIMS to detect 18-MEA in hair. [27][28][29][30] However, because we focused on quantitative comparisons, we chose XPS over TOF-SIMS for superior quantitative analysis. 31 In the XPS experiment, as the treatment time for hair damage increased, the area representing disul de decreased signi cantly, while the SO 3 − area slightly increased.…”

Section: Discussionmentioning

confidence: 99%

Biomimetics Through Bioconjugation of 16- Methylheptadecanoic Acid to Damaged Hair for Hair Barrier Recovery

Song,

Park,

Lim

et al. 2024

Preprint

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The primary component of the lipid barrier on human hair, which is essential for defense against aging and environmental stresses, is 18-methyleicosanoic acid (18-MEA), which provides hydrophobic properties and protective benefits. Since 18-MEA cannot be regenerated once damaged, it is critical to develop technology that can permanently bind alternativematerials to hair. Once it was determined that 18-MEA was removed from the hair using X-ray photoelectron spectroscopy (XPS), pentaerythritol tetraisoosterate (PTIS) was hydrolyzed and observed via gas chromatography/mass spectrometry (GC/MS)to confirm that mimic 18-MEA, 16-methylheptadecanoic acid (16-MHA) wasobtained at pH 4 or lower. The 16-MHA was bioconjugated to damaged hair from which 18-MEA was removed via a carbodiimide reaction using polycarbodiimide. Time-of-flight secondary ion mass spectrometry (TOF-SIMS) confirmed that 16-MHA remained on the surface of bioconjugated hair even after washing. Observation of the endothermic reaction of moisture in the hair using a differential scanning calorimeter (DSC) and evaluation of the moisture content confirmed that the hair bioconjugated with 16-MHA exhibited similar physical properties to virgin hair. This biomimetic approach has been demonstrated to restore both external structural integrity and internal moisture homeostasis.

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Section: Discussionmentioning

confidence: 99%

Biomimetics Through Bioconjugation of 16- Methylheptadecanoic Acid to Damaged Hair for Hair Barrier Recovery

Song,

Park,

Lim

et al. 2024

Preprint

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“…15,20,23–27 Protease, pectinase, and lipase carry out nucleophilic attacks on substrates containing structurally analogous Asp-His-Ser triads. 18,27–30 In contrast, catalase completes its catalytic cycle in two two-electron reductive and oxidative processes. 18,19,30–33…”

Section: Introductionmentioning

confidence: 99%

Cotton Dyeing with Sulfur Dyes using Alkaline Enzymes as Alternate Reducing Systems

Chakraborty¹,

Jaruhar²

2017

AATCC Journal of Research

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Sulfur dyes are water insoluble and require reduction as well as solubilization before application. These dyes are used for dyeing cotton with heavy shades, primarily because of good light and wash fastness at low cost. Sodium sulfide used for reduction is highly toxic, releasing sulfur products in drained out liquor, including hydrogen sulfide gas. Enzymes capable of reducing sulfur dyes were studied to replace sodium sulfide in dyebath formulations. It was found that a few enzymes viz. protease, pectinase, lipase, and catalase can effectively reduce all sulfur dyes. Dyebath potential, color strength (K/S), reduction bath stability, and colorfastness of dyeing were comparable among the reducing systems, thus demonstrating the feasibility of enzymatic cotton dyeing with sulfur dyes.

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“…Lipid removal could increase the amount of hydrophilic polar groups exposed on the wool surface, making the subsequent proteolytic reaction more efficient. Recently, enzymatic methods with lipase, thioesterase, and other esterases have been used to hydrolyze ester‐ and thioester‐bound fatty acids on the wool surface . Some scientists reported that lipase treatment improved the wettability of the wool fibers and enhanced the shrink resistance properties of the protease‐treated wool .…”

Section: Introductionmentioning

confidence: 99%

Bio‐antifelting of wool based on mild methanolic potassium hydroxide pretreatment

Wang

Yuan²,

Ren³

et al. 2012

Engineering in Life Sciences

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Covalently bound lipids cover the wool surface and make enzymatic degradation of wool scales very difficult. In this paper, methanolic potassium hydroxide (MPH) pretreatment was used prior to enzymatic treatment of wool with protease, aiming at hydrolyzing the outmost lipids on the wool surface and promoting the subsequent proteolytic reaction. The efficacy of lipid removal from the fiber surface and the properties of the protease‐treated wool were evaluated. The results indicated that mild MPH pretreatment with 0.10 mol/L MPH for 10 min improved the wettability of the wool without adverse impacts on its mechanical properties. The wetting time and area shrinkage of the wool fabric reached 0.5 s and 5.6%, respectively, and the strength loss was within the acceptable range. Pretreatment with high concentrations of MPH for longer times led to significant damage to the wool fibers and caused heavy strength loss, without improving the antifelting properties after protease treatment. Thus, the combination of mild MPH and protease treatments endowed the wool with desirable properties in contrast to the treatment with protease alone.

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Surface Chemical Analysis of Lipase Enzyme Treatments on Wool and Mohair

Cited by 16 publications

References 16 publications

Biomimetics Through Bioconjugation of 16- Methylheptadecanoic Acid to Damaged Hair for Hair Barrier Recovery

Biomimetics Through Bioconjugation of 16- Methylheptadecanoic Acid to Damaged Hair for Hair Barrier Recovery

Cotton Dyeing with Sulfur Dyes using Alkaline Enzymes as Alternate Reducing Systems

Bio‐antifelting of wool based on mild methanolic potassium hydroxide pretreatment

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