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Response Surface Methodology Modelling of an Aqueous Two-Phase System for Purification of Protease from Penicillium candidum (PCA 1/TT031) under Solid State Fermentation and Its Biochemical Characterization

Penicillium candidum (PCA 1/TT031) synthesizes different types of extracellular proteases. The objective of this study is to optimize polyethylene glycol (PEG)/citrate based on an aqueous two-phase system (ATPS) and Response Surface Methodology (RSM) to purify protease from Penicillium candidum (PCA... Full description

Journal Title: International Journal of Molecular Sciences 2016, Vol.17(11)
Main Author: Alhelli, Amaal
Other Authors: Manap, Mohd , Mohammed, Abdulkarim , Mirhosseini, Hamed , Suliman, Eilaf , Shad, Zahra , Mohammed, Nameer , Hussin, Anis
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 16616596 ; E-ISSN: 14220067 ; DOI: 10.3390/ijms17111872
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title: Response Surface Methodology Modelling of an Aqueous Two-Phase System for Purification of Protease from Penicillium candidum (PCA 1/TT031) under Solid State Fermentation and Its Biochemical Characterization
format: Article
creator:
  • Alhelli, Amaal
  • Manap, Mohd
  • Mohammed, Abdulkarim
  • Mirhosseini, Hamed
  • Suliman, Eilaf
  • Shad, Zahra
  • Mohammed, Nameer
  • Hussin, Anis
subjects:
  • Aqueous Chemistry
  • Fermentation
  • Proteases
  • Polyethylene Glycol
ispartof: International Journal of Molecular Sciences, 2016, Vol.17(11)
description: Penicillium candidum (PCA 1/TT031) synthesizes different types of extracellular proteases. The objective of this study is to optimize polyethylene glycol (PEG)/citrate based on an aqueous two-phase system (ATPS) and Response Surface Methodology (RSM) to purify protease from Penicillium candidum (PCA 1/TT031). The effects of different PEG molecular weights (1500-10,000 g/mol), PEG concentration (9%-20%), concentrations of NaCl (0%-10%) and the citrate buffer (8%-16%) on protease were also studied. The best protease purification could be achieved under the conditions of 9.0% (w/w) PEG 8000, 5.2% NaCl, and 15.9% sodium citrate concentration, which resulted in a one-sided protease partitioning for the bottom phase with a partition coefficient of 0.2, a 6.8-fold protease purification factor, and a yield of 93%. The response surface models displayed a significant (p ≤ 0.05) response which was fit for the variables that were studied as well as a high coefficient of determination (R2). Similarly,...
language: eng
source:
identifier: ISSN: 16616596 ; E-ISSN: 14220067 ; DOI: 10.3390/ijms17111872
fulltext: fulltext_linktorsrc
issn:
  • 16616596
  • 1661-6596
  • 14220067
  • 1422-0067
url: Link


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titleResponse Surface Methodology Modelling of an Aqueous Two-Phase System for Purification of Protease from Penicillium candidum (PCA 1/TT031) under Solid State Fermentation and Its Biochemical Characterization
creatorAlhelli, Amaal ; Manap, Mohd ; Mohammed, Abdulkarim ; Mirhosseini, Hamed ; Suliman, Eilaf ; Shad, Zahra ; Mohammed, Nameer ; Hussin, Anis
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subjectAqueous Chemistry ; Fermentation ; Proteases ; Polyethylene Glycol
descriptionPenicillium candidum (PCA 1/TT031) synthesizes different types of extracellular proteases. The objective of this study is to optimize polyethylene glycol (PEG)/citrate based on an aqueous two-phase system (ATPS) and Response Surface Methodology (RSM) to purify protease from Penicillium candidum (PCA 1/TT031). The effects of different PEG molecular weights (1500-10,000 g/mol), PEG concentration (9%-20%), concentrations of NaCl (0%-10%) and the citrate buffer (8%-16%) on protease were also studied. The best protease purification could be achieved under the conditions of 9.0% (w/w) PEG 8000, 5.2% NaCl, and 15.9% sodium citrate concentration, which resulted in a one-sided protease partitioning for the bottom phase with a partition coefficient of 0.2, a 6.8-fold protease purification factor, and a yield of 93%. The response surface models displayed a significant (p ≤ 0.05) response which was fit for the variables that were studied as well as a high coefficient of determination (R2). Similarly,...
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descriptionPenicillium candidum (PCA 1/TT031) synthesizes different types of extracellular proteases. The objective of this study is to optimize polyethylene glycol (PEG)/citrate based on an aqueous two-phase system (ATPS) and Response Surface Methodology (RSM) to purify protease from Penicillium candidum (PCA 1/TT031). The effects of different PEG molecular weights (1500-10,000 g/mol), PEG concentration (9%-20%), concentrations of NaCl (0%-10%) and the citrate buffer (8%-16%) on protease were also studied. The best protease purification could be achieved under the conditions of 9.0% (w/w) PEG 8000, 5.2% NaCl, and 15.9% sodium citrate concentration, which resulted in a one-sided protease partitioning for the bottom phase with a partition coefficient of 0.2, a 6.8-fold protease purification factor, and a yield of 93%. The response surface models displayed a significant (p ≤ 0.05) response which was fit for the variables that were studied as well as a high coefficient of determination (R2). Similarly,...
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authorAlhelli, Amaal ; Manap, Mohd ; Mohammed, Abdulkarim ; Mirhosseini, Hamed ; Suliman, Eilaf ; Shad, Zahra ; Mohammed, Nameer ; Hussin, Anis
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abstractPenicillium candidum (PCA 1/TT031) synthesizes different types of extracellular proteases. The objective of this study is to optimize polyethylene glycol (PEG)/citrate based on an aqueous two-phase system (ATPS) and Response Surface Methodology (RSM) to purify protease from Penicillium candidum (PCA 1/TT031). The effects of different PEG molecular weights (1500-10,000 g/mol), PEG concentration (9%-20%), concentrations of NaCl (0%-10%) and the citrate buffer (8%-16%) on protease were also studied. The best protease purification could be achieved under the conditions of 9.0% (w/w) PEG 8000, 5.2% NaCl, and 15.9% sodium citrate concentration, which resulted in a one-sided protease partitioning for the bottom phase with a partition coefficient of 0.2, a 6.8-fold protease purification factor, and a yield of 93%. The response surface models displayed a significant (p ≤ 0.05) response which was fit for the variables that were studied as well as a high coefficient of determination (R2). Similarly,...
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