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Truncated [alpha]-amylase: an improved candidate for textile processing
Enzymes are indispensable biocatalysts required in various steps of textile processing to minimize various chemical-induced hazards. The present work focuses on the applications of the truncated α-amylase in textile industry for desizing of fabrics by starch hydrolysis. The multiple sequence alignme...
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Published in: | Preparative biochemistry & biotechnology 2018-01, Vol.48 (7), p.635 |
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description | Enzymes are indispensable biocatalysts required in various steps of textile processing to minimize various chemical-induced hazards. The present work focuses on the applications of the truncated α-amylase in textile industry for desizing of fabrics by starch hydrolysis. The multiple sequence alignment was performed to find homology and the possible truncation region in Bacillus subtilis MTCC 121 α-amylase with same bacilli family α-amylase. Two constructs were generated for α-amylase gene of Bacillus subtilis MTCC 121 (Amy_F, full-length and Amy_T, C-terminal truncated) were cloned, overexpressed, purified, and characterized. Results revealed that activity of Amy_T was found to be 2.87-fold better than Amy_F. Further, the optimum temperature of Amy_F and Amy_T was obtained at 45 °C and 55 °C, respectively, whereas optimum pH was recorded at pH 7 and pH 8, respectively. Improved thermostability of Amy_T was further confirmed through thermal shift assay. Subsequently, starch-coated fabrics were tested for starch removal using the α-amylases. Comparative analysis revealed that Amy_T performed better in starch removal from polystyrene (85%), silk (75%), and cotton (70%) fabrics. The removal of starch from the fabrics was further confirmed by FESEM. Conclusively, this work presents one truncated α-amylase as an improved candidate over its full-length counterpart for textile desizing. |
doi_str_mv | 10.1080/10826068.2018.1479863 |
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The present work focuses on the applications of the truncated α-amylase in textile industry for desizing of fabrics by starch hydrolysis. The multiple sequence alignment was performed to find homology and the possible truncation region in Bacillus subtilis MTCC 121 α-amylase with same bacilli family α-amylase. Two constructs were generated for α-amylase gene of Bacillus subtilis MTCC 121 (Amy_F, full-length and Amy_T, C-terminal truncated) were cloned, overexpressed, purified, and characterized. Results revealed that activity of Amy_T was found to be 2.87-fold better than Amy_F. Further, the optimum temperature of Amy_F and Amy_T was obtained at 45 °C and 55 °C, respectively, whereas optimum pH was recorded at pH 7 and pH 8, respectively. Improved thermostability of Amy_T was further confirmed through thermal shift assay. Subsequently, starch-coated fabrics were tested for starch removal using the α-amylases. Comparative analysis revealed that Amy_T performed better in starch removal from polystyrene (85%), silk (75%), and cotton (70%) fabrics. The removal of starch from the fabrics was further confirmed by FESEM. Conclusively, this work presents one truncated α-amylase as an improved candidate over its full-length counterpart for textile desizing.</description><identifier>ISSN: 1082-6068</identifier><identifier>EISSN: 1532-2297</identifier><identifier>DOI: 10.1080/10826068.2018.1479863</identifier><language>eng</language><publisher>Philadelphia: Taylor & Francis Ltd</publisher><subject>Amylases ; Bacilli ; Bacillus subtilis ; Biocatalysts ; Comparative analysis ; Cotton ; Desizing ; Fabrics ; Hazards ; Homology ; Nucleotide sequence ; Organic chemistry ; pH effects ; Polystyrene ; Polystyrene resins ; Silk ; Starch ; Textile composites ; Textile industry ; Thermal stability ; α-Amylase</subject><ispartof>Preparative biochemistry & biotechnology, 2018-01, Vol.48 (7), p.635</ispartof><rights>2018 Taylor & Francis</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,778,782,27911,27912</link.rule.ids></links><search><creatorcontrib>Saha, Poulomi</creatorcontrib><creatorcontrib>Khan, Mohd Faheem</creatorcontrib><creatorcontrib>Patra, Sanjukta</creatorcontrib><title>Truncated [alpha]-amylase: an improved candidate for textile processing</title><title>Preparative biochemistry & biotechnology</title><description>Enzymes are indispensable biocatalysts required in various steps of textile processing to minimize various chemical-induced hazards. The present work focuses on the applications of the truncated α-amylase in textile industry for desizing of fabrics by starch hydrolysis. The multiple sequence alignment was performed to find homology and the possible truncation region in Bacillus subtilis MTCC 121 α-amylase with same bacilli family α-amylase. Two constructs were generated for α-amylase gene of Bacillus subtilis MTCC 121 (Amy_F, full-length and Amy_T, C-terminal truncated) were cloned, overexpressed, purified, and characterized. Results revealed that activity of Amy_T was found to be 2.87-fold better than Amy_F. Further, the optimum temperature of Amy_F and Amy_T was obtained at 45 °C and 55 °C, respectively, whereas optimum pH was recorded at pH 7 and pH 8, respectively. Improved thermostability of Amy_T was further confirmed through thermal shift assay. Subsequently, starch-coated fabrics were tested for starch removal using the α-amylases. Comparative analysis revealed that Amy_T performed better in starch removal from polystyrene (85%), silk (75%), and cotton (70%) fabrics. The removal of starch from the fabrics was further confirmed by FESEM. Conclusively, this work presents one truncated α-amylase as an improved candidate over its full-length counterpart for textile desizing.</description><subject>Amylases</subject><subject>Bacilli</subject><subject>Bacillus subtilis</subject><subject>Biocatalysts</subject><subject>Comparative analysis</subject><subject>Cotton</subject><subject>Desizing</subject><subject>Fabrics</subject><subject>Hazards</subject><subject>Homology</subject><subject>Nucleotide sequence</subject><subject>Organic chemistry</subject><subject>pH effects</subject><subject>Polystyrene</subject><subject>Polystyrene resins</subject><subject>Silk</subject><subject>Starch</subject><subject>Textile composites</subject><subject>Textile industry</subject><subject>Thermal stability</subject><subject>α-Amylase</subject><issn>1082-6068</issn><issn>1532-2297</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><recordid>eNotjUFLxDAUhIMouK7-BCHgOTXvvSZNvcmiq7Dgwb2JLGmaaJduW5tW9N8b0cvMwHzMMHYJMgNp5HUS1FKbDCWYDPKiNJqO2AIUoUAsi-OUEyN-oVN2FuNeSigLMAu23o5z5-zka_5i2-Hdvgp7-G5t9Dfcdrw5DGP_mUpnu7qpE8dDP_LJf01N63kqnY-x6d7O2UmwbfQX_75kz_d329WD2DytH1e3GzEA0CRK5TzlVueESEFVSlIdCk9Q5RY0lcZoa2ooXECTB3KOCsRaq-BRhYqW7OpvNR1_zD5Ou30_j1063CFonZsSAOkH4fxOPg</recordid><startdate>20180101</startdate><enddate>20180101</enddate><creator>Saha, Poulomi</creator><creator>Khan, Mohd Faheem</creator><creator>Patra, Sanjukta</creator><general>Taylor & Francis Ltd</general><scope>7QL</scope><scope>7QO</scope><scope>7QR</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope></search><sort><creationdate>20180101</creationdate><title>Truncated [alpha]-amylase: an improved candidate for textile processing</title><author>Saha, Poulomi ; Khan, Mohd Faheem ; Patra, Sanjukta</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p113t-95ce34a643223f5b503df7e31b4a1639886a8d17cf284f3cc3722d65fe25fb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Amylases</topic><topic>Bacilli</topic><topic>Bacillus subtilis</topic><topic>Biocatalysts</topic><topic>Comparative analysis</topic><topic>Cotton</topic><topic>Desizing</topic><topic>Fabrics</topic><topic>Hazards</topic><topic>Homology</topic><topic>Nucleotide sequence</topic><topic>Organic chemistry</topic><topic>pH effects</topic><topic>Polystyrene</topic><topic>Polystyrene resins</topic><topic>Silk</topic><topic>Starch</topic><topic>Textile composites</topic><topic>Textile industry</topic><topic>Thermal stability</topic><topic>α-Amylase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Saha, Poulomi</creatorcontrib><creatorcontrib>Khan, Mohd Faheem</creatorcontrib><creatorcontrib>Patra, Sanjukta</creatorcontrib><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Preparative biochemistry & biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Saha, Poulomi</au><au>Khan, Mohd Faheem</au><au>Patra, Sanjukta</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Truncated [alpha]-amylase: an improved candidate for textile processing</atitle><jtitle>Preparative biochemistry & biotechnology</jtitle><date>2018-01-01</date><risdate>2018</risdate><volume>48</volume><issue>7</issue><spage>635</spage><pages>635-</pages><issn>1082-6068</issn><eissn>1532-2297</eissn><abstract>Enzymes are indispensable biocatalysts required in various steps of textile processing to minimize various chemical-induced hazards. 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Comparative analysis revealed that Amy_T performed better in starch removal from polystyrene (85%), silk (75%), and cotton (70%) fabrics. The removal of starch from the fabrics was further confirmed by FESEM. Conclusively, this work presents one truncated α-amylase as an improved candidate over its full-length counterpart for textile desizing.</abstract><cop>Philadelphia</cop><pub>Taylor & Francis Ltd</pub><doi>10.1080/10826068.2018.1479863</doi></addata></record> |
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subjects | Amylases Bacilli Bacillus subtilis Biocatalysts Comparative analysis Cotton Desizing Fabrics Hazards Homology Nucleotide sequence Organic chemistry pH effects Polystyrene Polystyrene resins Silk Starch Textile composites Textile industry Thermal stability α-Amylase |
title | Truncated [alpha]-amylase: an improved candidate for textile processing |
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