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Partial purication and characterization of recombinant alkalne protease.

The thermostable protease which synthesized by using recombinant E.Coli is partially purified by using heat treatment at 70 C for10 .20 and 30 minutes. The enzyme which was purified for the duration of 30 minutes has lowest protein content and highest protease activity. The intracellular enzyme has...

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Main Author: Gayathri Selvaraju
Format: Undergraduate Final Project Report
Published: 2002
Online Access:http://discol.umk.edu.my/id/eprint/5569/
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spelling my.umk.eprints.55692022-05-23T08:42:05Z http://discol.umk.edu.my/id/eprint/5569/ Partial purication and characterization of recombinant alkalne protease. Gayathri Selvaraju The thermostable protease which synthesized by using recombinant E.Coli is partially purified by using heat treatment at 70 C for10 .20 and 30 minutes. The enzyme which was purified for the duration of 30 minutes has lowest protein content and highest protease activity. The intracellular enzyme has higher activity compared to the extracellular enzyme. The enzyme was partially purified 4-fold. The protein content of crude enzyme was higher than the partially purified enzyme. Yet. the enzyme activity of the partially purified enzyme is was higher than crude protease. SDS PAGE was carried out to confirm whether the sample is partially purified by observing the bands. The partially purified sample has lesser bands compared to the crude (control). Then, the characteristics that partially purified enzyme was studied. This enzyme has optimum temperature at 80 c with casein as substrate. Moreover, the optimum pH range is 8-10 but it could exhibit high activity at pH 10. Moreover. phenyl methane sulphonyl fluoride (PMSF) has inhibited the protease activity. But. it was not inhibited byth cEDaT_A÷:e a-Mercaptoethanol and SDS. in addition, the effect of metal ions was studied w_ +Z. Cu2`. Ag' and Fe' and Ca While, was able to increase the protease activity. 2 has little inhibitory effect on the protease activity but Cu2+, Ag` and Fe2 have high inhibitory effect on the protease activ\ty but they were not fully inhibited. 2002 Undergraduate Final Project Report NonPeerReviewed Gayathri Selvaraju (2002) Partial purication and characterization of recombinant alkalne protease. Undergraduate Final Project Report thesis, Faculty of Agro-Based Industry. (Submitted)
institution Universiti Malaysia Kelantan
building Perpustakaan Universiti Malaysia Kelantan
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Malaysia Kelantan
content_source UMK Institutional Repository
url_provider http://umkeprints.umk.edu.my/
description The thermostable protease which synthesized by using recombinant E.Coli is partially purified by using heat treatment at 70 C for10 .20 and 30 minutes. The enzyme which was purified for the duration of 30 minutes has lowest protein content and highest protease activity. The intracellular enzyme has higher activity compared to the extracellular enzyme. The enzyme was partially purified 4-fold. The protein content of crude enzyme was higher than the partially purified enzyme. Yet. the enzyme activity of the partially purified enzyme is was higher than crude protease. SDS PAGE was carried out to confirm whether the sample is partially purified by observing the bands. The partially purified sample has lesser bands compared to the crude (control). Then, the characteristics that partially purified enzyme was studied. This enzyme has optimum temperature at 80 c with casein as substrate. Moreover, the optimum pH range is 8-10 but it could exhibit high activity at pH 10. Moreover. phenyl methane sulphonyl fluoride (PMSF) has inhibited the protease activity. But. it was not inhibited byth cEDaT_A÷:e a-Mercaptoethanol and SDS. in addition, the effect of metal ions was studied w_ +Z. Cu2`. Ag' and Fe' and Ca While, was able to increase the protease activity. 2 has little inhibitory effect on the protease activity but Cu2+, Ag` and Fe2 have high inhibitory effect on the protease activ\ty but they were not fully inhibited.
format Undergraduate Final Project Report
author Gayathri Selvaraju
spellingShingle Gayathri Selvaraju
Partial purication and characterization of recombinant alkalne protease.
author_facet Gayathri Selvaraju
author_sort Gayathri Selvaraju
title Partial purication and characterization of recombinant alkalne protease.
title_short Partial purication and characterization of recombinant alkalne protease.
title_full Partial purication and characterization of recombinant alkalne protease.
title_fullStr Partial purication and characterization of recombinant alkalne protease.
title_full_unstemmed Partial purication and characterization of recombinant alkalne protease.
title_sort partial purication and characterization of recombinant alkalne protease.
publishDate 2002
url http://discol.umk.edu.my/id/eprint/5569/
_version_ 1763303571828244480
score 13.211869

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