• 한국염색가공학회지
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• 제26권4호
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• pp.283-289
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• 2014

This study describes the feasibility and optimization of reactive dyeing on bio treated cotton knitted fabrics. For this, cotton knitted fabrics distinctly with two different enzymes, alkaline Pectinases(Scourzyme $L^{(R)}$) and Pectate lyases(Bactosol Co. ip $liquor^{(R)}$). In this way by increasing the concentration and processing temperature, the access of enzymes towards the fatty and waxy substrate was found to be accelerated. To achieve higher absorbency and whiteness index, a series of experiments was carried out to assure that Pectate lyases enzymes possesses high access towards the fats and waxes at high temperature. To this end, cotton knitted fabrics was dyed without oxidative bleaching step. The Pectate lyases scoured and dyed fabrics showed less color difference when 2% dye shade is used. The fabrics pre-scoured with Pectate lyases showed good the light and washing fastness properties, compared to the conventional and Pectinases dyed fabrics. However pectinases enzymes showed lower activity at high temperature, caused poor wettability and whiteness index of fabrics. The improvement of the accessibility of enzyme to the pectin at higher temperature Pectate lyases treatment before dyeing was found to be useful for subsequent pectin degradation in cotton knitted fabrics.

• 미생물학회지
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• 제54권4호
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• pp.463-464
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• 2018

Tamlana sp. UJ94는 해수로부터 분리되었으며 알긴산을 분해할 수 있다. 알긴산 분해 관련 특성을 이해하기 위해 이 세균의 유전체를 분석하였다. UJ94의 유전체는 4,116,543 bp의크기로 3,609개의 코딩서열을 가지고 있으며 35.2 mol%의 G + C 함량을 가진다. BLASTp 검색 결과 9개의 alginate lyase 외에도 6개의 agarase, 5개의 amylase, 4개의 carrageenase, 1개의 cellulase, 4개의 pectate lyase, 7개의 xylanase의 존재가 예측되어 UJ94의 다양한 다당류 분해 능력을 암시하였다. Tamlana sp. UJ94의 유전체는 생물전환 공정에 사용할 수 있는 다당류 분해 유전자를 제공할 수 있을 것이다.

• Journal of Microbiology and Biotechnology
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• 제20권4호
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• pp.670-677
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• 2010

An alkaline pectate lyase, Bsp165PelA, was purified to homogeneity from the culture broth of alkaliphilic Bacillus sp. N16-5. The enzyme showed a specific activity as high as 1,000 U/mg and had optimum activity at pH 11.5 and $50^{\circ}C$. It was composed of a single polypeptide chain with a molecular mass of 42 kDa deduced from SDS-PAGE, and its isoelectric point was around pH 6.0. It could efficiently depolymerize polygalacturonate and pectin. Characterization of product formation revealed unsaturated digalacturonate and trigalacturonate as the main products. The pectate lyase gene (pelA) contained an open reading frame (ORF) of 1,089 bp, encoding a 36-amino acids signal peptide and a mature protein of 326 amino acids with a calculated molecular mass of 35.943 Da. The deduced amino acid sequence from the pelA ORF exhibited significant homology to those of known pectate lyases in polysaccharide lyase family 1. Some conserved active-site amino acids were found in the deduced amino acid sequence of Bsp165PelA. $Ca^{2+}$ was not required for activity on pectic substrates.