High-level extracellular production of an alkaline pectate lyase in E. coli BL21 (DE3) and its application in bioscouring of cotton fabric
A high heterologous expression of an alkaline pectate lyase (APL) pelNK93I in E. coli was obtained through optimizing the lactose feeding and fed-batch fermentation. The highest soluble APL activity produced by E. coli BL21 (pET22b-pelNK93I) was 10,181 U/mL which is the highest level so far. On this basis, to improve the extracellular yield of APL, optimized glycine feeding was used to achieve elevated extracellular production of pelNK93I. The highest extracellular APL activity produced by E. coli BL21 (pET22b-pelNK93I) was 6357 U/mL which was also relatively higher than that in previous reports. The final productivity of APL was 282.8 U/mL/h in the fermentation of E. coli BL21 (pET22b-pelNK93I) in a 10 L fermenter. Thus the current study has provided a cost-effective method for the over-expression and preparation of alkaline pectate lyase pelNK93I for its industrial applications. Moreover, pelNK93I (4 U/mL) used for bioscouring increased cottonseed husk removal and radial capillary effect of cotton fabric by 37.63% and 47.06%, respectively, making it a promising enzyme in green textile technology.
KeywordspelNK93I Fed-batch fermentation Glycine feeding Cottonseed husk removal Enzymatic pretreatment
The authors thank Dr. Zhanping Zhou and Jiangning Song for their kind donation of the strain E. coli BL21 (pET22b-pelNK93I). This work was financially supported by the National Natural Science Fund of China (Grant 31701534), the Tianjin outstanding talent training program, the Tianjin Science and Technology Planning Project (Grant 14ZCZDSY00157 and 15PTCYSY00020) and Yantai Marine economy innovation development demonstration project (Grant YHCX-SW-L-201703).
Compliance with ethical standards
Conflict of interest
The authors have declared no conflict of interest.
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