Optimization of serine protease purification from mango (Mangifera indica Cv. Chokanan) peel in polyethylene glycol/ dextran aqueous two phase system
Mango peel is a good source of protease but remains an industrial waste. This study focuses on the optimization of PEG/Dextran-based aqueous two-phase system ATPS) to purify serine protease from mango peel. The activity of serine protease in different phase systems was studied and then the possible...
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iium-179782016-12-15T07:22:53Z http://irep.iium.edu.my/17978/ Optimization of serine protease purification from mango (Mangifera indica Cv. Chokanan) peel in polyethylene glycol/ dextran aqueous two phase system Mehrnoush, Amid Mustafa, Shuhaimi Sarker, Md. Zaidul Islam Mohd Yazid, Abdul Manap QD Chemistry Mango peel is a good source of protease but remains an industrial waste. This study focuses on the optimization of PEG/Dextran-based aqueous two-phase system ATPS) to purify serine protease from mango peel. The activity of serine protease in different phase systems was studied and then the possible relationship between the purification variables, namely polyethylene glycol molecular weight (PEG, 4000-12,000 g mol-1), tie line length (-3.42-35.27%), NaCl (-2.5-11.5%) and pH (4.5-10.5) on the enzymatic properties of purified enzyme was investigated. The most significant effect of PEG was on the efficiency of serine protease purification. Also, there was a significant increase in the partition coefficient with the addition of 4.5% of NaCl to the system. This could be due to the high hydrophobicity of serine protease compared to protein contaminates. The optimum conditions to achieve high partition coefficient (84.2) purification factor (14.37) and yield (97.3%) of serine protease were obtained in the presence of 8000 g mol-1 of PEG, 17.2% of tie line length and 4.5% of NaCl at pH 7.5. The enzymatic properties of purified serine protease using PEG/dextran ATPS showed that the enzyme could be purified at a high level of purification factor and yield with easy scale-up and fast processing. MDPI 2012 Article PeerReviewed application/pdf en http://irep.iium.edu.my/17978/1/Intl_J_Mol_Sci.pdf application/pdf en http://irep.iium.edu.my/17978/4/Optimization_of_Serine_Protease_Purification_from_Mango_%28Mangifera_indica_cv._Chokanan%29_Peel_in_Polyethylene_GlycolDextran_Aqueous_Two_Phase_System.pdf Mehrnoush, Amid and Mustafa, Shuhaimi and Sarker, Md. Zaidul Islam and Mohd Yazid, Abdul Manap (2012) Optimization of serine protease purification from mango (Mangifera indica Cv. Chokanan) peel in polyethylene glycol/ dextran aqueous two phase system. International Journal of Molecular Sciences, 13. pp. 3636-3649. ISSN 1422-0067 http://www.mdpi.com/journal/ijms doi:10.3390/ijms13033636 |
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QD Chemistry Mehrnoush, Amid Mustafa, Shuhaimi Sarker, Md. Zaidul Islam Mohd Yazid, Abdul Manap Optimization of serine protease purification from mango (Mangifera indica Cv. Chokanan) peel in polyethylene glycol/ dextran aqueous two phase system |
description |
Mango peel is a good source of protease but remains an industrial waste. This study focuses on the optimization of PEG/Dextran-based aqueous two-phase system ATPS) to purify serine protease from mango peel. The activity of serine protease in different phase systems was studied and then the possible relationship between the purification variables, namely polyethylene glycol molecular weight (PEG, 4000-12,000 g mol-1), tie line length (-3.42-35.27%), NaCl (-2.5-11.5%) and pH (4.5-10.5) on the enzymatic properties of purified enzyme was investigated. The most significant effect of PEG was on the efficiency of serine protease purification. Also, there was a significant increase in the partition coefficient with the addition of 4.5% of NaCl to the system. This could be due to the high hydrophobicity of serine protease compared to protein contaminates. The optimum conditions to achieve high partition coefficient (84.2) purification factor (14.37) and yield (97.3%) of serine protease were obtained in the presence of 8000 g mol-1 of PEG, 17.2% of tie line length and 4.5% of NaCl at pH 7.5. The enzymatic properties of purified serine protease using PEG/dextran ATPS showed that the enzyme could be purified at a high level of purification factor and yield with easy scale-up and fast processing. |
format |
Article |
author |
Mehrnoush, Amid Mustafa, Shuhaimi Sarker, Md. Zaidul Islam Mohd Yazid, Abdul Manap |
author_facet |
Mehrnoush, Amid Mustafa, Shuhaimi Sarker, Md. Zaidul Islam Mohd Yazid, Abdul Manap |
author_sort |
Mehrnoush, Amid |
title |
Optimization of serine protease purification from mango (Mangifera indica Cv. Chokanan) peel in polyethylene glycol/ dextran aqueous two phase system |
title_short |
Optimization of serine protease purification from mango (Mangifera indica Cv. Chokanan) peel in polyethylene glycol/ dextran aqueous two phase system |
title_full |
Optimization of serine protease purification from mango (Mangifera indica Cv. Chokanan) peel in polyethylene glycol/ dextran aqueous two phase system |
title_fullStr |
Optimization of serine protease purification from mango (Mangifera indica Cv. Chokanan) peel in polyethylene glycol/ dextran aqueous two phase system |
title_full_unstemmed |
Optimization of serine protease purification from mango (Mangifera indica Cv. Chokanan) peel in polyethylene glycol/ dextran aqueous two phase system |
title_sort |
optimization of serine protease purification from mango (mangifera indica cv. chokanan) peel in polyethylene glycol/ dextran aqueous two phase system |
publisher |
MDPI |
publishDate |
2012 |
url |
http://irep.iium.edu.my/17978/ http://irep.iium.edu.my/17978/ http://irep.iium.edu.my/17978/ http://irep.iium.edu.my/17978/1/Intl_J_Mol_Sci.pdf http://irep.iium.edu.my/17978/4/Optimization_of_Serine_Protease_Purification_from_Mango_%28Mangifera_indica_cv._Chokanan%29_Peel_in_Polyethylene_GlycolDextran_Aqueous_Two_Phase_System.pdf |
first_indexed |
2023-09-18T20:27:01Z |
last_indexed |
2023-09-18T20:27:01Z |
_version_ |
1777408484283777024 |