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Cocoa pod husk, a new source of hydrolase enzymes for preparation of cross-linked enzyme aggregate
Cocoa pod husk (CPH) is a by-product of cocoa production obtained after removing the beans from the fruit. The analysis of CPH has shown that it contains high amounts of protein. This study is aimed to utilize this protein source in hydrolase enzyme production. In this study, seven hydrolase enzymes...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer International Publishing
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4750640/ https://www.ncbi.nlm.nih.gov/pubmed/26904389 http://dx.doi.org/10.1186/s40064-015-1621-3 |
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author | Yusof, Faridah Khanahmadi, Soofia Amid, Azura Mahmod, Safa Senan |
author_facet | Yusof, Faridah Khanahmadi, Soofia Amid, Azura Mahmod, Safa Senan |
author_sort | Yusof, Faridah |
collection | PubMed |
description | Cocoa pod husk (CPH) is a by-product of cocoa production obtained after removing the beans from the fruit. The analysis of CPH has shown that it contains high amounts of protein. This study is aimed to utilize this protein source in hydrolase enzyme production. In this study, seven hydrolase enzymes (amylase, fructosyltransferase, mannanase, glucosidase, glucanase, lipase and protease) were screened from CPH for the first time for feasible industrial production. Among these hydrolases, lipase was chosen for the next steps of experiments as it has a lot of applications in different industries. The extraction of high active lipase from CPH has been done under optimum conditions. The condition that was optimum for the three major factors was achieved using Face centered central composite design (FCCCD) with response surface methodology (RSM) to obtain the highest enzyme activity of crude lipase from CPH. The optimum condition of extraction is used for preparation of cross-linked enzyme aggregate (CLEA). For the production of immobilized biocatalyst, the technique of CLEA is considered as an effective technique for its industrially attractive advantages. Referring to the results of OFAT, CLEA-lipase was prepared in the best condition at the presence of 30 mM ammonium sulphate, 70 mM glutaraldehyde with 0.23 mM Bovine serum albumin as an additive. Immobilization effectively improved the stability of lipase against various organic solvents. |
format | Online Article Text |
id | pubmed-4750640 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Springer International Publishing |
record_format | MEDLINE/PubMed |
spelling | pubmed-47506402016-02-22 Cocoa pod husk, a new source of hydrolase enzymes for preparation of cross-linked enzyme aggregate Yusof, Faridah Khanahmadi, Soofia Amid, Azura Mahmod, Safa Senan Springerplus Research Cocoa pod husk (CPH) is a by-product of cocoa production obtained after removing the beans from the fruit. The analysis of CPH has shown that it contains high amounts of protein. This study is aimed to utilize this protein source in hydrolase enzyme production. In this study, seven hydrolase enzymes (amylase, fructosyltransferase, mannanase, glucosidase, glucanase, lipase and protease) were screened from CPH for the first time for feasible industrial production. Among these hydrolases, lipase was chosen for the next steps of experiments as it has a lot of applications in different industries. The extraction of high active lipase from CPH has been done under optimum conditions. The condition that was optimum for the three major factors was achieved using Face centered central composite design (FCCCD) with response surface methodology (RSM) to obtain the highest enzyme activity of crude lipase from CPH. The optimum condition of extraction is used for preparation of cross-linked enzyme aggregate (CLEA). For the production of immobilized biocatalyst, the technique of CLEA is considered as an effective technique for its industrially attractive advantages. Referring to the results of OFAT, CLEA-lipase was prepared in the best condition at the presence of 30 mM ammonium sulphate, 70 mM glutaraldehyde with 0.23 mM Bovine serum albumin as an additive. Immobilization effectively improved the stability of lipase against various organic solvents. Springer International Publishing 2016-01-20 /pmc/articles/PMC4750640/ /pubmed/26904389 http://dx.doi.org/10.1186/s40064-015-1621-3 Text en © Yusof et al. 2016 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. |
spellingShingle | Research Yusof, Faridah Khanahmadi, Soofia Amid, Azura Mahmod, Safa Senan Cocoa pod husk, a new source of hydrolase enzymes for preparation of cross-linked enzyme aggregate |
title | Cocoa pod husk, a new source of hydrolase
enzymes for preparation of cross-linked enzyme aggregate |
title_full | Cocoa pod husk, a new source of hydrolase
enzymes for preparation of cross-linked enzyme aggregate |
title_fullStr | Cocoa pod husk, a new source of hydrolase
enzymes for preparation of cross-linked enzyme aggregate |
title_full_unstemmed | Cocoa pod husk, a new source of hydrolase
enzymes for preparation of cross-linked enzyme aggregate |
title_short | Cocoa pod husk, a new source of hydrolase
enzymes for preparation of cross-linked enzyme aggregate |
title_sort | cocoa pod husk, a new source of hydrolase
enzymes for preparation of cross-linked enzyme aggregate |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4750640/ https://www.ncbi.nlm.nih.gov/pubmed/26904389 http://dx.doi.org/10.1186/s40064-015-1621-3 |
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