Please use this identifier to cite or link to this item: http://nopr.niscpr.res.in/handle/123456789/19264
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dc.contributor.authorEl-Ola, Samiha M Abo-
dc.contributor.authorMoharam, Maysa E-
dc.contributor.authorEl-Bendary, Magda A-
dc.date.accessioned2013-06-20T13:55:19Z-
dc.date.available2013-06-20T13:55:19Z-
dc.date.issued2013-06-
dc.identifier.issn0975-1025 (Online); 0971-0426 (Print)-
dc.identifier.urihttp://hdl.handle.net/123456789/19264-
dc.description165-172en_US
dc.description.abstractThe optimum conditions for surface modification of polyethylene terephthalate (PET) by lipase enzymes produced under economic conditions by two Egyptian bacilli (Bacillus isolate 6C and Bacillus isolate 5W) have been obtained and then compared with reference sample. The optimum conditions are found to be 0.04 mg/mL enzyme concentration, 0.5 h incubation time, room temperature (25 ºC) and pH 8 under shaking conditions. Addition of 0.15% CaCl2 to the treatment bath enhances both the hydrophilicity (18-26%) and dyeability (22- 194%). The effect of hydrolytic activity of enzymatic process on the weight loss after treatment does not show any significant difference. Printing both untreated and treated PET fabrics with transfer printing shows high leveling properties w.r.t. ∆E values, where it is considered as acceptable values of color differences. PET treated with different sources of lipase enzyme under optimum conditions shows good physical properties and high water regain. SEM of the surface of lipase treated PET samples shows cracks and voids compared to smooth surface of untreated PET fabrics. en_US
dc.language.isoen_USen_US
dc.publisherNISCAIR-CSIR, Indiaen_US
dc.rightsCC Attribution-Noncommercial-No Derivative Works 2.5 Indiaen_US
dc.sourceIJFTR Vol.38(2) [June 2013]en_US
dc.subjectEgyptian bacillien_US
dc.subjectLipase enzymeen_US
dc.subjectPhysical propertiesen_US
dc.subjectPoly(ethylene terephthalate)en_US
dc.subjectSurface modificationsen_US
dc.subjectTransfer printingen_US
dc.titleOptimum conditions for surface modification of PET by lipase enzymes produced by Egyptian bacilli in comparison with standard oneen_US
dc.typeArticleen_US
Appears in Collections:IJFTR Vol.38(2) [June 2013]

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