王冬伟,孙谧.固载化木聚糖酶交联酶聚集体的制备及性质D[J].中国海洋药物,2016,35(1):39-49. |
固载化木聚糖酶交联酶聚集体的制备及性质D |
The preparation and properties of the immobilized Xylanase by carrier-crosslinked enzyme aggregation |
投稿时间:2015-07-01 修订日期:2015-08-30 |
DOI: |
中文关键词: 木聚糖酶 交联酶聚集体 固定化 酶学性质 |
English Keywords:Xylanase immobilized CLEAs enzymatic properties |
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中文摘要: |
目的 提高木聚糖酶YS1069的稳定性、重复利用率以及便于从反应体系中分离。方法 本文将交联酶聚集体CLEAs技术与载体固定化技术相结合,用LKZ-128氨基型树脂对木聚糖酶CLEAs进行固定化,并对其性质进行初步研究。结果及结论 采用单因素法和响应面法对影响固定化酶活性的因素进行分析和优化,获得最佳固定化条件为: pH 9.0的酶液,以2 mL的异丙醇为沉淀剂,沉淀1 h,以1.59 g/L的京尼平为交联剂,交联2 h,20 ℃的环境中固定化9.25 h,加酶量为8 mg时回收率最高,达到65.63%,加酶量为60 mg时酶活性最高,达到190 U/g。重复使用10次后,其相对酶活仍为42.3%,说明具有良好的批次操作稳定性。该酶经过固定化后热稳定性和pH稳定性均得到了提高。 |
English Summary: |
Objective Enhance the stability, repeated utilization of Xylanase and easily separated from the reaction system. Methods In this study, the cross-linked enzyme aggregates (CLEAs) technology combined with carrier immobilization technique. Using amino resin LKZ-128 immbolized Xylanase CLEAs and studying its properties. Results and Conclusion Immobilized conditions of Xylanase CLEAs were studied by using single factor experiment and the response surface design. The study indicated that the best immobilized conditions were: pH 9.0 enzyme liquid precipitated by 2 mL isopropyl, precipitation 1 h, and crosslinked 2 h with the carrier LKZ-128 by 1.59 g/L genipin. ImmobilizedS9.25ShSinStheSenvironmentSofS20 ℃. The recovery rate up to 65.63% when the enzyme dosage was 8 mg, and activity of enzyme up to 190 U/g when the enzyme dosage was 60 mg. After repeated 10 times, the relative activity of the enzyme is still 42.3%, Sshowing goodSreusability. Thermal stability and pH stability of the enzyme were improved after Immobilized. |
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