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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Main Authors: CHENG, YUNG- HSI, 鄭永熙
Other Authors: LEE, CHUNG-YI
Format: Others
Language:zh-TW
Published: 2016
Online Access:http://ndltd.ncl.edu.tw/handle/60457770619322476339
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spelling 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
collection NDLTD
language zh-TW
format Others
sources NDLTD
description 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.
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
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AT chengyunghsi alterococcusagarolyticuss3pynàirèdàfēnziyángcàiméichúnhuàyǔdìngxìng
AT zhèngyǒngxī alterococcusagarolyticuss3pynàirèdàfēnziyángcàiméichúnhuàyǔdìngxìng
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