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作 者:刘春琴[1] 余养盛[1] 白钢[1] 杨文博[1] 陈宁[2] 怀立华[2]
机构地区:[1]南开大学生命科学学院,天津300071 [2]天津科技大学生物工程学院,天津300222
出 处:《微生物学通报》2008年第1期45-49,共5页Microbiology China
基 金:国家自然科学基金资助项目(No.30470053);天津市重点基金资助项目(No.05YFJZJC00900)
摘 要:对以DL-2-氨基-△^2-噻唑啉-4-羧酸(DL-2-amino-A2thiazoline-4-carboxylic acid,DL—ATC)为底物原料,经微生物酶法催化合成L-半胱氨酸,并进一步氧化和分离纯化产物L-胱氨酸的生产工艺和条件进行了研究。建立了以恶臭假单胞菌TS1138(Pseudomonas putida TS1138)全细胞为酶源,反复多次催化底物合成L-半胱氨酸,并以2.0%二甲基亚砜(DMSO)为氧化剂氧化生成L-胱氨酸,进而通过001×7型阳离子交换树脂纯化胱氨酸的新工艺。采用高效液相色谱法考察该方法L-胱氨酸的总收率可以达到78.55%,纯度为99.12%。该方法简单高效,解决了酶稳定性差不能重复使用,而固定化酶方法繁琐成本高的问题,为我国L-半胱氨酸和L-胱氨酸的生产开辟一条新途径。A technology of L-cystine production was studied in this paper, which included microbial enzymatic conversion of DL-2-amino-△^2-thiazoline-4-carboxylic acid (DL-ATC) to L-cysteine, subsequent oxidization of L-cysteine to L-cystine and its purification. The cells of Pseudomonas putida TS 1138 could be repetitively used as the enzyme sources to convert the substrate DL-ATC to L-cysteine. After being oxidated by 2% dimethy-sulforide (DMSO), L-cystine could be harvested and further purified by the positive ion-exchange resin 001×7. High Performance Liquid Chromatography (HPLC) identified the purified L-cystine as having a total recovery of 78.55% and purity of 99.12%. This study demonstrated an efficient and convenient method for L-cystine production, which overcame the instability of enzymes, troublesome procedures and high cost of enzyme immobilization as contrasted to the traditional method. All in all, it provides a new approach for industrial production of L-cystine as well as L-cysteine.
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