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Continuous degradation of maltose by enzyme entrapment technology using calcium alginate beads as a matrix
Maltase from Bacillus licheniformis KIBGE-IB4 was immobilized within calcium alginate beads using entrapment technique. Immobilized maltase showed maximum immobilization yield with 4% sodium alginate and 0.2 M calcium chloride within 90.0 min of curing time. Entrapment increases the enzyme–substrate...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5669356/ https://www.ncbi.nlm.nih.gov/pubmed/29124211 http://dx.doi.org/10.1016/j.bbrep.2015.09.025 |
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author | Nawaz, Muhammad Asif Rehman, Haneef Ur Bibi, Zainab Aman, Afsheen Ul Qader, Shah Ali |
author_facet | Nawaz, Muhammad Asif Rehman, Haneef Ur Bibi, Zainab Aman, Afsheen Ul Qader, Shah Ali |
author_sort | Nawaz, Muhammad Asif |
collection | PubMed |
description | Maltase from Bacillus licheniformis KIBGE-IB4 was immobilized within calcium alginate beads using entrapment technique. Immobilized maltase showed maximum immobilization yield with 4% sodium alginate and 0.2 M calcium chloride within 90.0 min of curing time. Entrapment increases the enzyme–substrate reaction time and temperature from 5.0 to 10.0 min and 45 °C to 50 °C, respectively as compared to its free counterpart. However, pH optima remained same for maltose hydrolysis. Diffusional limitation of substrate (maltose) caused a declined in V(max) of immobilized enzyme from 8411.0 to 4919.0 U ml(−1) min(−1) whereas, K(m) apparently increased from 1.71 to 3.17 mM ml(−1). Immobilization also increased the stability of free maltase against a broad temperature range and enzyme retained 45% and 32% activity at 55 °C and 60 °C, respectively after 90.0 min. Immobilized enzyme also exhibited recycling efficiency more than six cycles and retained 17% of its initial activity even after 6th cycles. Immobilized enzyme showed relatively better storage stability at 4 °C and 30 °C after 60.0 days as compared to free enzyme. |
format | Online Article Text |
id | pubmed-5669356 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-56693562017-11-09 Continuous degradation of maltose by enzyme entrapment technology using calcium alginate beads as a matrix Nawaz, Muhammad Asif Rehman, Haneef Ur Bibi, Zainab Aman, Afsheen Ul Qader, Shah Ali Biochem Biophys Rep Research Article Maltase from Bacillus licheniformis KIBGE-IB4 was immobilized within calcium alginate beads using entrapment technique. Immobilized maltase showed maximum immobilization yield with 4% sodium alginate and 0.2 M calcium chloride within 90.0 min of curing time. Entrapment increases the enzyme–substrate reaction time and temperature from 5.0 to 10.0 min and 45 °C to 50 °C, respectively as compared to its free counterpart. However, pH optima remained same for maltose hydrolysis. Diffusional limitation of substrate (maltose) caused a declined in V(max) of immobilized enzyme from 8411.0 to 4919.0 U ml(−1) min(−1) whereas, K(m) apparently increased from 1.71 to 3.17 mM ml(−1). Immobilization also increased the stability of free maltase against a broad temperature range and enzyme retained 45% and 32% activity at 55 °C and 60 °C, respectively after 90.0 min. Immobilized enzyme also exhibited recycling efficiency more than six cycles and retained 17% of its initial activity even after 6th cycles. Immobilized enzyme showed relatively better storage stability at 4 °C and 30 °C after 60.0 days as compared to free enzyme. Elsevier 2015-10-08 /pmc/articles/PMC5669356/ /pubmed/29124211 http://dx.doi.org/10.1016/j.bbrep.2015.09.025 Text en © 2015 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Research Article Nawaz, Muhammad Asif Rehman, Haneef Ur Bibi, Zainab Aman, Afsheen Ul Qader, Shah Ali Continuous degradation of maltose by enzyme entrapment technology using calcium alginate beads as a matrix |
title | Continuous degradation of maltose by enzyme entrapment technology using calcium alginate beads as a matrix |
title_full | Continuous degradation of maltose by enzyme entrapment technology using calcium alginate beads as a matrix |
title_fullStr | Continuous degradation of maltose by enzyme entrapment technology using calcium alginate beads as a matrix |
title_full_unstemmed | Continuous degradation of maltose by enzyme entrapment technology using calcium alginate beads as a matrix |
title_short | Continuous degradation of maltose by enzyme entrapment technology using calcium alginate beads as a matrix |
title_sort | continuous degradation of maltose by enzyme entrapment technology using calcium alginate beads as a matrix |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5669356/ https://www.ncbi.nlm.nih.gov/pubmed/29124211 http://dx.doi.org/10.1016/j.bbrep.2015.09.025 |
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