Phospholipase D(PLD)is an essential biocatalyst for the biological production of phosphatidylserine and phospholipid modification.However,the efficient heterologous expression of PLD is limited by its cell toxicity.In...Phospholipase D(PLD)is an essential biocatalyst for the biological production of phosphatidylserine and phospholipid modification.However,the efficient heterologous expression of PLD is limited by its cell toxicity.In this study,a PLD was secretory expressed efficiently in Bacillus subtilis with an activity around 100 U/mL.A secretory expression system containing the signal peptide SPEstA and the dual-promoter PHpaII-SrfA was estab-lished,and the extracellular PLD activity further reached 119.22 U/mL through scale-up fermentation,191.30-fold higher than that of the control.Under optimum reaction conditions,a 61.61%conversion ratio and 21.07 g/L of phosphatidylserine production were achieved.Finally,the synthesis system of PL derivates was established,which could efficiently synthesis novel PL derivates.The results highlight that the secretory expression system constructed in this study provides a promising PLD producing strain in industrial application,and laid the foundation for the biosynthesis of phosphatidylserine and other PL derivates.As far as we know,this work re-ports the highest level of extracellular PLD expression to date and the enzymatic production of several PL der-ivates for the first time.展开更多
W_(18)O_(49)nanowires(W_(18)O_(49)NWs)with unique one-dimension structures and excellent electron/ions transport properties have attracted increasing attention in academia and industry because of their potential appli...W_(18)O_(49)nanowires(W_(18)O_(49)NWs)with unique one-dimension structures and excellent electron/ions transport properties have attracted increasing attention in academia and industry because of their potential applications in many energy-related devices.In the past decades,many research articles related to W_(18)O_(49)have been published,but there are insufficient review articles focusing on W_(18)O_(49)NWs.In this review,we present the crystal structure of W_(18)O_(49)and briefly introduce the synthesis methods and growth mechanism of W_(18)O_(49)NWs.Moreover,their applications in energy conversion and storage devices are summarized.Finally,the current challenges and opportunities for applying W_(18)O_(49)NWs are provided.We hope this review can promote the development of W_(18)O_(49)NWs in energy conversion,storage,and other promising applications.展开更多
Trehalose is a non-reducing disaccharide connected byα-1,1-glycosidic bonds;it is widely distributed in bacteria,fungi,yeast,insects,and plant tissues and plays various roles.It can be hydrolyzed by trehalase into tw...Trehalose is a non-reducing disaccharide connected byα-1,1-glycosidic bonds;it is widely distributed in bacteria,fungi,yeast,insects,and plant tissues and plays various roles.It can be hydrolyzed by trehalase into two glucose molecules.Trehalases from different sources have been expressed in Escherichia coli,Pichia pastoris,Saccharomyces cerevisiae,baculovirus-silkworm,and other expression systems;however,it is most common in E.coli.The structural characteristics of different glycoside hydrolase(GH)family trehalases and the sources of trehalase have been analyzed.The catalytic mechanism of GH37 trehalase has also been elucidated in detail.Moreover,the molecular modification of trehalase has mainly focused on directed evolution for improving enzyme activity.We comprehensively reviewed the current application status and adaptable transformations was comprehensively overviewed in the context of industrial performance.We suggest that the level of recombinant production is far from meeting industrial requirements,and the catalytic performance of trehalase needs to be improved urgently.Finally,we discuss developmental prospects and future trends.展开更多
基金supported by the National Key Research and Development Program of China(No.2021YFC2100900)the National Natural Science Foundation of China(No.32171261)+1 种基金the Natural Science Foundation of Jiangsu Province(No.BK20221082)the Fundamental Research Funds for the Central Universities(No.JUSRP21940).
文摘Phospholipase D(PLD)is an essential biocatalyst for the biological production of phosphatidylserine and phospholipid modification.However,the efficient heterologous expression of PLD is limited by its cell toxicity.In this study,a PLD was secretory expressed efficiently in Bacillus subtilis with an activity around 100 U/mL.A secretory expression system containing the signal peptide SPEstA and the dual-promoter PHpaII-SrfA was estab-lished,and the extracellular PLD activity further reached 119.22 U/mL through scale-up fermentation,191.30-fold higher than that of the control.Under optimum reaction conditions,a 61.61%conversion ratio and 21.07 g/L of phosphatidylserine production were achieved.Finally,the synthesis system of PL derivates was established,which could efficiently synthesis novel PL derivates.The results highlight that the secretory expression system constructed in this study provides a promising PLD producing strain in industrial application,and laid the foundation for the biosynthesis of phosphatidylserine and other PL derivates.As far as we know,this work re-ports the highest level of extracellular PLD expression to date and the enzymatic production of several PL der-ivates for the first time.
基金Financial support from the National Natural Science Foundation(No.22075151)of Chinathe Natural Science Foundation of Jiangxi(No.20161BBE50095)the project of Jiangxi Academy of Sciences(No.2022YSBG21019 and No.2023YJC2018)is gratefully acknowledged。
文摘W_(18)O_(49)nanowires(W_(18)O_(49)NWs)with unique one-dimension structures and excellent electron/ions transport properties have attracted increasing attention in academia and industry because of their potential applications in many energy-related devices.In the past decades,many research articles related to W_(18)O_(49)have been published,but there are insufficient review articles focusing on W_(18)O_(49)NWs.In this review,we present the crystal structure of W_(18)O_(49)and briefly introduce the synthesis methods and growth mechanism of W_(18)O_(49)NWs.Moreover,their applications in energy conversion and storage devices are summarized.Finally,the current challenges and opportunities for applying W_(18)O_(49)NWs are provided.We hope this review can promote the development of W_(18)O_(49)NWs in energy conversion,storage,and other promising applications.
基金Project supported by the National First-Class Discipline Program of Light Industry Technology and Engineering(Nos.LITE2018-18 and LITE2018-11) of Chinathe Transformation Project for Major Scientific and Technological Achievements in Jiangsu Province(No.BA2015006)+1 种基金the Industry-Academia Cooperation Innovation Fund Project of Jiangsu Province(No.BY2016022-19)the National Key Technologies R&D Program of China for the 12th Five-year Plan(No.2012BAD33B06)
基金supported by the National Key Research and Development Program of China(No.2021YFC2102000)the National Natural Science Foundation of China(No.21978116 and 32171261)the Ningxia Hui Autonomous Region Key Research&Development Plan(No.2019BCH01002).
文摘Trehalose is a non-reducing disaccharide connected byα-1,1-glycosidic bonds;it is widely distributed in bacteria,fungi,yeast,insects,and plant tissues and plays various roles.It can be hydrolyzed by trehalase into two glucose molecules.Trehalases from different sources have been expressed in Escherichia coli,Pichia pastoris,Saccharomyces cerevisiae,baculovirus-silkworm,and other expression systems;however,it is most common in E.coli.The structural characteristics of different glycoside hydrolase(GH)family trehalases and the sources of trehalase have been analyzed.The catalytic mechanism of GH37 trehalase has also been elucidated in detail.Moreover,the molecular modification of trehalase has mainly focused on directed evolution for improving enzyme activity.We comprehensively reviewed the current application status and adaptable transformations was comprehensively overviewed in the context of industrial performance.We suggest that the level of recombinant production is far from meeting industrial requirements,and the catalytic performance of trehalase needs to be improved urgently.Finally,we discuss developmental prospects and future trends.