Catalog | ACMA00029798 |
Description | It is a concentrated bacterial alpha amylase for desizing of cotton fabrics sized with starch derivatives and blends of starch |
Solubility | Dissolves into water in every percentage |
Storage | Like all enzyme products, it slowly loses activity over time. To ensure maximum storage life and activity th product should be stored at 25°C or lower temperature. Higher storage temperature should be avoided. Stir well before use for optimum results, store in a cool place with containers tightly closed. |
Composition | Based on alpha-amylase |
Feature | Eco- friendly. Allows rapid conversion of the starch size into dextrin, which is easily removed by rinsing following impregnation of the enzyme. Midium temperature stable. Effective in wide operating temperatures and pH. |
Form | Brown, liquid |
Ionicity | Anionic |
pH | 5.5 ± 0.5 |
Type | Desizing Enzymes |
Hao, Longyun, et al. Carbohydrate polymers, 2013, 96(2), 474-480.
The textile industry employs two main clean technology methods for desizing which are enzymatic processing using α-amylase and ultrasound irradiation. In the present work, with the aim of giving a further insight to the influence of ultrasound on α-amylase activity and its desizing efficiency, the ultrasound-based experiments were afforded in two ways: The study explored two distinct procedures for desizing cotton fabric with α-amylase: (i) treating the fabric in stages with ultrasound followed by enzymatic desizing and (ii) applying both ultrasound and α-amylase simultaneously during desizing.
· The step-wise procedure demonstrates that ultrasound negatively affects -amylase activity with soluble starch as the substrate. Sonicated -amylase demonstrates superior desizing efficiency because ultrasound leads to increased hydrophobic interactions between sonicated amylase and its substrate through amino acid unfolding which reveals hydrophobic regions and enhances catalytic action on insoluble starch. The sonicated amylase shows a 2-3 nm red-shift in its maximum fluorescence emission wavelength.
· The simultaneous procedure produces a stronger improvement in desizing efficiency compared to the step-wise procedure. Through ultrasonic assistance, desizing quality can be achieved at a 10 ◦C lower operating temperature compared to conventional methods. The observed results stem from multiple reasons including better stirring/mixing performance and substrate damage or alteration together with improved catalysis in hydrolytic reactions and quicker elimination of loosened substances from fabric bulk.
Madhu, Amit, et al. Research Journal of Textile and Apparel, 2018, 22(3), 271-290.
The traditional approach to starch size removal utilizes α-amylase enzymes because it is both conventional and environmentally friendly. After finishing the process enzymes are conventionally drained because as catalysts they stay active beyond the reaction and require recycling. Immobilization enables enzyme recovery to deploy them effectively as practical biocatalysts. This research works to recover α-amylase for cotton fabric desizing through immobilization techniques.
· Methodology
This research examined how α-amylase immobilized on Chitosan and a synthetic soluble-insoluble copolymer of methacrylic acid and methyl methacrylate operates to remove size from cotton fabrics. Researchers immobilized commercial α-amylase onto polymers that alternate between soluble and insoluble states to address challenges presented by heterogeneous reaction media. The process of immobilization was optimized to achieve maximum conjugate activity which enabled the use of immobilized amylases in the desizing of grey cotton fabrics.
· Key Findings
The performance of immobilized amylases during desizing was assessed based on their ability to remove starch and compared with results from free enzyme. Immobilized amylases maintained sufficient desizing efficiency through four cycles of operation and allowed simple recovery after each cycle. The efficiency of amylase immobilized on copolymer exceeds that of chitosan at specific concentrations.
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