生物加工过程
生物加工過程
생물가공과정
CHINESE JOURNAL OF BIOPROCESS ENGINEERING
2014年
2期
12-16
,共5页
胡集铖%王欢%李亚%韩萍芳
鬍集鋮%王歡%李亞%韓萍芳
호집성%왕환%리아%한평방
凹凸棒石黏土%固定化%介孔%猪胰脂肪酶%超顺磁性
凹凸棒石黏土%固定化%介孔%豬胰脂肪酶%超順磁性
요철봉석점토%고정화%개공%저이지방매%초순자성
attapulgite%immobilization%mesoporous%porcine pancreatic lipase%superparamagnetic
以凹凸棒石黏土为原料,制备γ Fe2 O3凹土超顺磁性纳米复合材料(γ Fe2 O3 ATP )作为猪胰脂肪酶(PPL)固定化的载体,利用透射电子显微镜(TEM)、N2吸附脱附等温图(BET)、振动试样磁强计(VSM)等对材料进行表征,同时对固定化条件和固定化酶的相关性质进行了研究。结果表明:制备的γ Fe2 O3 ATP是介孔材料,比表面积为.63 m2/g,平均孔径为.862 nm,饱和磁化强度为.915 emu/g,其作为载体能实现固定化酶与反应介质简单、快速分离回收和重复利用。在固定化时间为h及pH6.0时制备的固定化酶效果最佳;经过h高温保存后固定化酶可保留初始酶活的%,而游离酶仅保留初始酶活的%,同时固定化酶在重复使用次后酶活仍保留初始酶活的%。
以凹凸棒石黏土為原料,製備γ Fe2 O3凹土超順磁性納米複閤材料(γ Fe2 O3 ATP )作為豬胰脂肪酶(PPL)固定化的載體,利用透射電子顯微鏡(TEM)、N2吸附脫附等溫圖(BET)、振動試樣磁彊計(VSM)等對材料進行錶徵,同時對固定化條件和固定化酶的相關性質進行瞭研究。結果錶明:製備的γ Fe2 O3 ATP是介孔材料,比錶麵積為.63 m2/g,平均孔徑為.862 nm,飽和磁化彊度為.915 emu/g,其作為載體能實現固定化酶與反應介質簡單、快速分離迴收和重複利用。在固定化時間為h及pH6.0時製備的固定化酶效果最佳;經過h高溫保存後固定化酶可保留初始酶活的%,而遊離酶僅保留初始酶活的%,同時固定化酶在重複使用次後酶活仍保留初始酶活的%。
이요철봉석점토위원료,제비γ Fe2 O3요토초순자성납미복합재료(γ Fe2 O3 ATP )작위저이지방매(PPL)고정화적재체,이용투사전자현미경(TEM)、N2흡부탈부등온도(BET)、진동시양자강계(VSM)등대재료진행표정,동시대고정화조건화고정화매적상관성질진행료연구。결과표명:제비적γ Fe2 O3 ATP시개공재료,비표면적위.63 m2/g,평균공경위.862 nm,포화자화강도위.915 emu/g,기작위재체능실현고정화매여반응개질간단、쾌속분리회수화중복이용。재고정화시간위h급pH6.0시제비적고정화매효과최가;경과h고온보존후고정화매가보류초시매활적%,이유리매부보류초시매활적%,동시고정화매재중복사용차후매활잉보류초시매활적%。
The porcine pancreatic lipase( PPL) was immobilized on superparamagnetic γ-Fe2O3-attapulgite nanocomposites ( γ-Fe2 O3-ATP ) . The γ-Fe2 O3-ATP was characterized with transmission election microscopy ( TEM ) , BET and VSM. The immobilization conditions and enzymatic properties of immobilized PPL were investigated. The results showed that the γ-Fe2 O3-ATP was mesoporous material,specific surface area was 102.63 m2/g,average pore diameter was 10.862 nm, and saturation magnetization was 8.915 emu/g. The optimal immobilization conditions were determined to be pH 6.0 and immobilization time was 4 h. The thermal stability of the immobilized enzyme was enhanced compared with the free enzyme. The residual activity was kept at 52% for 6 h, while that of the free enzyme was just 19%. The catalytic activity of immobilized enzyme was kept at 60% after 5 batch reactions. Enzymes supported on superparamagnetic γ-Fe2O3-ATP could be easily separated and reused.