Encapsulation of multi-enzymes on waste clay material: preparation, characterization and application for tapioca starch hydrolysis
Alpha-amylase, glucoamylase and cellulase were immobilized onto calcium alginate-waste clay (alg-WC) beads by using encapsulation technique. The clay was obtained from palm oil mill clay bath processing waste that was collected from FELDA Serting Hilir Palm Oil Mill, Malaysia. The aim of this study...
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2014
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my.upm.eprints.374352016-09-08T01:31:59Z http://psasir.upm.edu.my/id/eprint/37435/ Encapsulation of multi-enzymes on waste clay material: preparation, characterization and application for tapioca starch hydrolysis Edama, Nurul Aini Sulaiman, Alawi Ku Hamid, Ku Halim Abd Rahim, Siti Noraida Samsu Baharuddin, Azhari Mokhtar, Mohd Noriznan Alpha-amylase, glucoamylase and cellulase were immobilized onto calcium alginate-waste clay (alg-WC) beads by using encapsulation technique. The clay was obtained from palm oil mill clay bath processing waste that was collected from FELDA Serting Hilir Palm Oil Mill, Malaysia. The aim of this study is to characterize and investigate the performance of waste clay as a supporting material for the tapioca starch hydrolysis. The encapsulated enzymes were characterized by using analytical equipment such as Fourier Transform Infrared Spectroscopy (FTIR) and Field Emission Scanning Electron Microscopy (FESEM). The FTIR results showed the interaction of functional groups between alginate and waste clay in the alg-WC beads. The alginate beads characterized at peaks 1615 cm-1, 1417 cm-1 and 1027 cm-1, and peaks 1396 cm-1, 873 cm-1 and 712 cm-1 characterized the waste clay. The FESEM analysis also revealed that the different surface morphology of alginate beads and alg-WC beads. It also showed that the enzymes were successfully encapsulated within the alg-WC beads. The activity of the immobilized enzymes was studied at different clay concentrations. The highest immobilization yield was obtained at 2% (w/v) of clay concentration and the highest enzyme loading was 98.29 %. The immobilized enzymes also retained 33% of its activity after seven usage cycle with 1 hour of each reaction time. Trans Tech Publications 2014 Article PeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/37435/1/Encapsulation%20of%20multi-enzymes%20on%20waste%20clay%20material%20Preparation%2C%20characterization%20and%20application%20for%20tapioca%20starch%20hydrolysis.pdf Edama, Nurul Aini and Sulaiman, Alawi and Ku Hamid, Ku Halim and Abd Rahim, Siti Noraida and Samsu Baharuddin, Azhari and Mokhtar, Mohd Noriznan (2014) Encapsulation of multi-enzymes on waste clay material: preparation, characterization and application for tapioca starch hydrolysis. Applied Mechanics and Materials, 548-549. pp. 77-82. ISSN 1660-9336; ESSN: 1662-7482 http://www.scientific.net/AMM.548-549.77 10.4028/www.scientific.net/AMM.548-549.77 |
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Alpha-amylase, glucoamylase and cellulase were immobilized onto calcium alginate-waste clay (alg-WC) beads by using encapsulation technique. The clay was obtained from palm oil mill clay bath processing waste that was collected from FELDA Serting Hilir Palm Oil Mill, Malaysia. The aim of this study is to characterize and investigate the performance of waste clay as a supporting material for the tapioca starch hydrolysis. The encapsulated enzymes were characterized by using analytical equipment such as Fourier Transform Infrared Spectroscopy (FTIR) and Field Emission Scanning Electron Microscopy (FESEM). The FTIR results showed the interaction of functional groups between alginate and waste clay in the alg-WC beads. The alginate beads characterized at peaks 1615 cm-1, 1417 cm-1 and 1027 cm-1, and peaks 1396 cm-1, 873 cm-1 and 712 cm-1 characterized the waste clay. The FESEM analysis also revealed that the different surface morphology of alginate beads and alg-WC beads. It also showed that the enzymes were successfully encapsulated within the alg-WC beads. The activity of the immobilized enzymes was studied at different clay concentrations. The highest immobilization yield was obtained at 2% (w/v) of clay concentration and the highest enzyme loading was 98.29 %. The immobilized enzymes also retained 33% of its activity after seven usage cycle with 1 hour of each reaction time. |
format |
Article |
author |
Edama, Nurul Aini Sulaiman, Alawi Ku Hamid, Ku Halim Abd Rahim, Siti Noraida Samsu Baharuddin, Azhari Mokhtar, Mohd Noriznan |
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Edama, Nurul Aini Sulaiman, Alawi Ku Hamid, Ku Halim Abd Rahim, Siti Noraida Samsu Baharuddin, Azhari Mokhtar, Mohd Noriznan Encapsulation of multi-enzymes on waste clay material: preparation, characterization and application for tapioca starch hydrolysis |
author_facet |
Edama, Nurul Aini Sulaiman, Alawi Ku Hamid, Ku Halim Abd Rahim, Siti Noraida Samsu Baharuddin, Azhari Mokhtar, Mohd Noriznan |
author_sort |
Edama, Nurul Aini |
title |
Encapsulation of multi-enzymes on waste clay material: preparation, characterization and application for tapioca starch hydrolysis |
title_short |
Encapsulation of multi-enzymes on waste clay material: preparation, characterization and application for tapioca starch hydrolysis |
title_full |
Encapsulation of multi-enzymes on waste clay material: preparation, characterization and application for tapioca starch hydrolysis |
title_fullStr |
Encapsulation of multi-enzymes on waste clay material: preparation, characterization and application for tapioca starch hydrolysis |
title_full_unstemmed |
Encapsulation of multi-enzymes on waste clay material: preparation, characterization and application for tapioca starch hydrolysis |
title_sort |
encapsulation of multi-enzymes on waste clay material: preparation, characterization and application for tapioca starch hydrolysis |
publisher |
Trans Tech Publications |
publishDate |
2014 |
url |
http://psasir.upm.edu.my/id/eprint/37435/1/Encapsulation%20of%20multi-enzymes%20on%20waste%20clay%20material%20Preparation%2C%20characterization%20and%20application%20for%20tapioca%20starch%20hydrolysis.pdf http://psasir.upm.edu.my/id/eprint/37435/ http://www.scientific.net/AMM.548-549.77 |
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1643831983457959936 |
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13.211869 |