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芽孢杆菌发酵产碱性果胶酶温度控制策略 被引量:4

APPLICATION OF A TWO-STAGE TEMPERATURE CONTROL STRATEGY FOR ALKALINE PECTATE LYASE PRODUCTION IN BATCH FERMENTATION BY BACILLUS SP.
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摘要 采用自行筛选获得一株产碱性果胶酶芽孢杆菌WSH03-09,在小型发酵罐中研究了不同温度对碱性果胶酶分批发酵的影响.结果表明,在恒定39℃条件下,可获得最高酶活5.39u/mL,各温度条件下的菌体干重相差不多,最终均能达11.5g/L左右;在发酵前期,控制温度41℃时最有利于菌体的生长,而在产物合成期,控制37℃有利于获得较高的产物合成比速.在此基础上,提出分阶段温度控制策略,采用此温度控制策略进行碱性果胶酶的发酵,碱性果胶酶酶活达5.99u/mL,比采用单一温度下的最大值提高了11%,其它各项指标也有较大提高. Alkaline pectate lyase can be used to degrade pectin around cotton fibres in textile industry for improving quality of cotton fabrics and environment by replacing traditional chemical agents, so it is crucial to get high productivity of pectate lyase by fermentation. Temperature is one of the most important factors affecting the yield and productivity of pectate lyase. In this study, the effect of different temperatures from 35 ℃ to 41℃ in a 7 L stirred fermenter was studied. An increase in pectate lyase production was obtained at higher temperature (39 ℃), while no obvious difference in dry cell weight was observed at different temperatures. Base on the results that the maximal specific cell growth rate could be achieved in 2 h at 41℃ and the higher specific pectate lyase production rate in product formation phase was at 37 ℃, a two-stage temperature control strategy was proposed. As a result, pectate lyase activity reached 5.99 u/mL and was increased by 31%, 11% and 43%, compared to single temperatures at 37 ℃, 39 ℃ and 41 ℃, respectively. Fig 6, Tab 1, Ref 6
出处 《应用与环境生物学报》 CAS CSCD 北大核心 2005年第3期359-362,共4页 Chinese Journal of Applied and Environmental Biology
基金 国家高技术研究发展计划(国家"863"计划)(2003AA322050)~~
关键词 芽孢杆菌 碱性果胶酶 分段温度控制 分批发酵 Bacillus sp. alkaline pectate lyase two-stage temperature control batch fermentation
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  • 1Etters JN, Husain PA, Lange NK. Alkaline pectinase: an eco-friendly approach to cotton preparation. Textile Asia, 1999, 5:83 ~85
  • 2Sakamoto T, Hours BA, Sakai T. Purification, characterization, and production of two pectic transeliminases with protopectinase activity from Bacillus subtilis. Biosci Biotech Biochem, 1994, 58 (2): 353 ~358
  • 3Kobayashi T, Koike K, Yoshimatsu T, et al. Purification and properties of a low-molecular-weight, high-alkaline pectate lyase from an alkaliphilic strain of Bacillus. Biosc Biotech Biochem, 1999, 63 (1): 65 ~ 72
  • 4Takao M, Nakaniwa T, Yoshikawa K, et al. Purification and characterization of thermostable pectate lyase with protopectinase activity from thermophilic Bacillus sp. TS 47. Biosci Biotech Biochem, 2000, 64(11): 2360 ~ 2367
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  • 6HuangWK(黄伟昆).TestandAnalysisofFood,Beijing(北京)[M].Chinese Light Industry Press(中国轻工业出版社),1991..

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