Purification and Characterization of Thermostable High Molecular Weight Agarase from Alterococcus Agarolyticus S3PY
碩士 === 東吳大學 === 微生物學系 === 104 === The agarolytic bacterium Alterococcus agarolyticus S3PY was isolated from hot spring in Ludao by our laboratory. Previous research revealed that product are multiple agarases, they were of the opinion that it caused by protease. This study confirmed the presence of...
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ndltd-TW-104SCU003810062016-10-14T04:10:28Z http://ndltd.ncl.edu.tw/handle/60457770619322476339 Purification and Characterization of Thermostable High Molecular Weight Agarase from Alterococcus Agarolyticus S3PY Alterococcus agarolyticus S3PY 耐熱大分子洋菜酶純化與定性 CHENG, YUNG- HSI 鄭永熙 碩士 東吳大學 微生物學系 104 The agarolytic bacterium Alterococcus agarolyticus S3PY was isolated from hot spring in Ludao by our laboratory. Previous research revealed that product are multiple agarases, they were of the opinion that it caused by protease. This study confirmed the presence of protease, and it can be inhibited by EDTA. In this research, high molecular weight agarase can be obtained in fermenter culture without aeration and after purification in the presence of EDTA. A new thermostable 53kDa-agarase was found after purification with ion exchange column. The 53kDa-agarase has high thermal stability that retained approximately 99 % of the initial activity after incubation for 1 hour at 60 ℃, and retained 83 % activity after 12 hours. LEE, CHUNG-YI 李重義 2016 學位論文 ; thesis 77 zh-TW |
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碩士 === 東吳大學 === 微生物學系 === 104 === The agarolytic bacterium Alterococcus agarolyticus S3PY was isolated from hot spring in Ludao by our laboratory. Previous research revealed that product are multiple agarases, they were of the opinion that it caused by protease. This study confirmed the presence of protease, and it can be inhibited by EDTA. In this research, high molecular weight agarase can be obtained in fermenter culture without aeration and after purification in the presence of EDTA. A new thermostable 53kDa-agarase was found after purification with ion exchange column. The 53kDa-agarase has high thermal stability that retained approximately 99 % of the initial activity after incubation for 1 hour at 60 ℃, and retained 83 % activity after 12 hours.
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author2 |
LEE, CHUNG-YI |
author_facet |
LEE, CHUNG-YI CHENG, YUNG- HSI 鄭永熙 |
author |
CHENG, YUNG- HSI 鄭永熙 |
spellingShingle |
CHENG, YUNG- HSI 鄭永熙 Purification and Characterization of Thermostable High Molecular Weight Agarase from Alterococcus Agarolyticus S3PY |
author_sort |
CHENG, YUNG- HSI |
title |
Purification and Characterization of Thermostable High Molecular Weight Agarase from Alterococcus Agarolyticus S3PY |
title_short |
Purification and Characterization of Thermostable High Molecular Weight Agarase from Alterococcus Agarolyticus S3PY |
title_full |
Purification and Characterization of Thermostable High Molecular Weight Agarase from Alterococcus Agarolyticus S3PY |
title_fullStr |
Purification and Characterization of Thermostable High Molecular Weight Agarase from Alterococcus Agarolyticus S3PY |
title_full_unstemmed |
Purification and Characterization of Thermostable High Molecular Weight Agarase from Alterococcus Agarolyticus S3PY |
title_sort |
purification and characterization of thermostable high molecular weight agarase from alterococcus agarolyticus s3py |
publishDate |
2016 |
url |
http://ndltd.ncl.edu.tw/handle/60457770619322476339 |
work_keys_str_mv |
AT chengyunghsi purificationandcharacterizationofthermostablehighmolecularweightagarasefromalterococcusagarolyticuss3py AT zhèngyǒngxī purificationandcharacterizationofthermostablehighmolecularweightagarasefromalterococcusagarolyticuss3py AT chengyunghsi alterococcusagarolyticuss3pynàirèdàfēnziyángcàiméichúnhuàyǔdìngxìng AT zhèngyǒngxī alterococcusagarolyticuss3pynàirèdàfēnziyángcàiméichúnhuàyǔdìngxìng |
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1718386855044448256 |