When it concerns optimising biochemical processes in food and its allied industries, evaluating the inactivation kinetic model of an enzyme is germane for their acceptable use. Thermal inactivation kinetics of amylase obtained from Bacillus sp. sourced from soil in a Cassava processing site were conducted in this study. Thermal inactivation of the amylase was examined in detail between 40 and 90°C within a specific time frame. This study suggests the possibility of the enzyme structure having a non-sensitive heat fraction, whose stability based on the enzyme activity was evident up to temperatures close to 70ºC. Denaturation of amylase was measured by loss in enzyme activity, which could be described as a first-order monophasic kinetic model, with k-values between 9 ×10-5 to 1.2 ×10-3 min-1. Also, D- and k-values decreased and increased, respectively, with soaring temperature, indicating swift amylase inactivation at higher temperatures. Results suggested that amylase is a relatively thermostable enzyme with a Z-value of 47.39°C and Ea of 24.51 kJmol-1. The high values obtained for activation energy (Ea), change in enthalpy (ΔH) which is 21.7 kJ/mol, indicated that a considerably large amount of energy will be needed to denature this amylase, possible due to its stable molecular conformation. Hence, the enzyme is relatively stable for biotechnological applications.
| Published in | Science Frontiers (Volume 4, Issue 4) |
| DOI | 10.11648/j.sf.20230404.11 |
| Page(s) | 48-53 |
| Creative Commons |
This is an Open Access article, 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 or format, provided the original work is properly cited. |
| Copyright |
Copyright © The Author(s), 2023. Published by Science Publishing Group |
Kinetic Studies, Thermodynamics, Thermal Inactivation, Amylase, Bacillus sp., Cassava
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APA Style
Oluwasegun Victor Omotoyinbo. (2023). Exploring the Kinetic and Thermodynamic Profiles of Amylase Thermal Inactivation Derived from Bacillus sp.. Science Frontiers, 4(4), 48-53. https://doi.org/10.11648/j.sf.20230404.11
ACS Style
Oluwasegun Victor Omotoyinbo. Exploring the Kinetic and Thermodynamic Profiles of Amylase Thermal Inactivation Derived from Bacillus sp.. Sci. Front. 2023, 4(4), 48-53. doi: 10.11648/j.sf.20230404.11
AMA Style
Oluwasegun Victor Omotoyinbo. Exploring the Kinetic and Thermodynamic Profiles of Amylase Thermal Inactivation Derived from Bacillus sp.. Sci Front. 2023;4(4):48-53. doi: 10.11648/j.sf.20230404.11
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Download@article{10.11648/j.sf.20230404.11,
author = {Oluwasegun Victor Omotoyinbo},
title = {Exploring the Kinetic and Thermodynamic Profiles of Amylase Thermal Inactivation Derived from Bacillus sp.},
journal = {Science Frontiers},
volume = {4},
number = {4},
pages = {48-53},
doi = {10.11648/j.sf.20230404.11},
url = {https://doi.org/10.11648/j.sf.20230404.11},
eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.sf.20230404.11},
abstract = {When it concerns optimising biochemical processes in food and its allied industries, evaluating the inactivation kinetic model of an enzyme is germane for their acceptable use. Thermal inactivation kinetics of amylase obtained from Bacillus sp. sourced from soil in a Cassava processing site were conducted in this study. Thermal inactivation of the amylase was examined in detail between 40 and 90°C within a specific time frame. This study suggests the possibility of the enzyme structure having a non-sensitive heat fraction, whose stability based on the enzyme activity was evident up to temperatures close to 70ºC. Denaturation of amylase was measured by loss in enzyme activity, which could be described as a first-order monophasic kinetic model, with k-values between 9 ×10-5 to 1.2 ×10-3 min-1. Also, D- and k-values decreased and increased, respectively, with soaring temperature, indicating swift amylase inactivation at higher temperatures. Results suggested that amylase is a relatively thermostable enzyme with a Z-value of 47.39°C and Ea of 24.51 kJmol-1. The high values obtained for activation energy (Ea), change in enthalpy (ΔH) which is 21.7 kJ/mol, indicated that a considerably large amount of energy will be needed to denature this amylase, possible due to its stable molecular conformation. Hence, the enzyme is relatively stable for biotechnological applications.},
year = {2023}
}
TY - JOUR T1 - Exploring the Kinetic and Thermodynamic Profiles of Amylase Thermal Inactivation Derived from Bacillus sp. AU - Oluwasegun Victor Omotoyinbo Y1 - 2023/10/08 PY - 2023 N1 - https://doi.org/10.11648/j.sf.20230404.11 DO - 10.11648/j.sf.20230404.11 T2 - Science Frontiers JF - Science Frontiers JO - Science Frontiers SP - 48 EP - 53 PB - Science Publishing Group SN - 2994-7030 UR - https://doi.org/10.11648/j.sf.20230404.11 AB - When it concerns optimising biochemical processes in food and its allied industries, evaluating the inactivation kinetic model of an enzyme is germane for their acceptable use. Thermal inactivation kinetics of amylase obtained from Bacillus sp. sourced from soil in a Cassava processing site were conducted in this study. Thermal inactivation of the amylase was examined in detail between 40 and 90°C within a specific time frame. This study suggests the possibility of the enzyme structure having a non-sensitive heat fraction, whose stability based on the enzyme activity was evident up to temperatures close to 70ºC. Denaturation of amylase was measured by loss in enzyme activity, which could be described as a first-order monophasic kinetic model, with k-values between 9 ×10-5 to 1.2 ×10-3 min-1. Also, D- and k-values decreased and increased, respectively, with soaring temperature, indicating swift amylase inactivation at higher temperatures. Results suggested that amylase is a relatively thermostable enzyme with a Z-value of 47.39°C and Ea of 24.51 kJmol-1. The high values obtained for activation energy (Ea), change in enthalpy (ΔH) which is 21.7 kJ/mol, indicated that a considerably large amount of energy will be needed to denature this amylase, possible due to its stable molecular conformation. Hence, the enzyme is relatively stable for biotechnological applications. VL - 4 IS - 4 ER -
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