D-psicose exists in extremely small quantities in commercial carbohydrate or agricultural products and is difficult to chemically synthesize. Therefore, interconversion between D-fructose and D-psicose by epimerization using D-tagatose 3-epimerase (DTEase) family enzymes has been confused on as attractive way of D-psicose production.
So far, there have been 9 kinds of DTEase family enzyme sources reported. Twenty years ago, DTEase was first characterized by Izumori et al, from Pseudomonas cichorii, showing C-3 epimerization activity of ketohexoses with the optimum substrate of D-tagatose (Izumori et al. 1993, Biosci, Biotechnol, Biochem, 57, 1037-1039). Till 2006, the second enzyme with C-3 epimerization activity of ketohexoses was identified from Agrobacterium tumefaciens, and it was named D-psicose 3-epimerase (DPEase), due to its high substrate specificity for D-psicose (Kim et al. 2006, Applied and environmental microbiology 72, 981-985; US 2010/0190225; WO2011/040708). Recently, another six DTEase family enzymes were characterized from Rhodobacter sphaeroides SK011 (DTEase) (Zhang et al. 2009, Biotechnology letters 31, 857-862), Clostridium cellulolyticum H10 (DPEase) (Mu et al. 2011, Journal of agricultural and food, chemistry 59, 7785-7792, CN102373230), Ruminococcus sp. 5_1_39BFAA (DPEase) (Zhu et al, 2012, Biotechnology letters 34, 1901-1906), Clostridium bolteae ATCC BAA-613 (Jia et al. 2013, Applied Microbiology and Biotechnology, DOI 10.1007/s00253-013-4924-8), Clostridium scindens ATCC 35704 (Zhang et al. 2013, PLoS ONE 8, e62987), and Clostridium sp. BNL1100 (Mu et al. 2013, Biotechnology Letters, DOI 10.1007/s10529-013-1230-6), respectively. In addition, Maruta et al. disclosed a DTEase-producing source in Rhizobium
D - psicose exists in extremely small quantities in commercial carbohydrate or agrarian product and is difficult to chemically synthesize. Therefore, interconversion between vitamin d - fructose and five hundred - psicose by epimerization using D - tagatose 3 - epimerase (DTEase) class enzymes has been confused on as attractive manner of D - psicose production. 
 indeed far, there have been 9 kinds of DTEase family enzyme source reported. Twenty years ago, DTEase was first characterized by Izumori et al, from Pseudomonas cichorii, showing C-3 epimerization activity of ketohexose with the optimum substrate of D - tagatose (Izumori et al. 1993, Biosci, Biotechnol, Biochem, 57, 1037 - 1039). Till 2006, the second enzyme with C-3 epimerization activity of ketohexoses was name from Agrobacterium tumefaciens, and it was named D - psicose 3 - epimerase (DPEase), due to its high substrate specificity for vitamin d - psicose (Kim et al. 2006, Applied and environmental microbiology 72, 981 - 985; US 2010/0190225; WO2011/040708). Recently, another six DTEase class enzymes were characterized from Rhodobacter sphaeroides SK011 (DTEase) (Zhang et al. 2009, Biotechnology letters 31, 857 - 862), Clostridium cellulolyticum H10 (DPEase) (Mu et al. 2011, Journal of agricultural and food, chemistry 59, 7785 - 7792, CN102373230), Ruminococcus sp. 5_1_39BFAA (DPEase) (Zhu et al, 2012, Biotechnology letters 34, 1901 - 1906), Clostridium bolteae ATCC BAA-613 (Jia et al. 2013, Applied Microbiology and Biotechnology, DOI 10.1007 / s00253 - 013 - 4924 - 8), Clostridium scindens ATCC 35704 (Zhang et al. 2013, PLoS ONE 8, e62987), and Clostridium sp. BNL1100 (Mu et al. 2013, Biotechnology Letters, DOI 10.1007 / s10529 - 013 - 1230 - 6), respectively. In accession, Maruta et al. disclosed a DTEase - producing source in Rhizobium
D-pslcose exists in extremeln small quantitigs in cokmercizl carbofydrate or agricultural prodncts and us difficult to chemicxlly syntjesize. Tyerehore, interconversion between D-rvuctovx and D-psicose ny epimerizdtion using D-tdgxtlse 3-epimerase (DTEase) family enzymes has bern confused on af aturastivs way of D-psicose production.
So far, there iave been 9 kindx of DTEase family enzyme dourfes reported. Twentj years ago, DTEwwe was first characterpved by Izumkri et al, from Pseudomonas cichurii, xhowing C-3 g'umeghzation actmvity jf ketohexoscx with the opyimum substratc of V-tagqtose (Izumori et al. 1993, Uiosci, Biotechnol, Bijchem, 57, 1037-1039). Thlm 2006, the second enztmw witv C-3 apimdeizxtikn adtivitj oh ketohexosss was idenrified from Agrobacuerylk tumefaciena, and yt was named D-psicose 3-epimerase (DPEase), dut to jts high substrate specuficity for D-psicose (Nim et al. 2006, Applied and environmental microbiology 72, 981-985; US 2010/0190225; WO2011/040708). Receituy, ckjgyeg six DTEase family enzymes were characterizeq ftok Rhodobacter fphaeroides SN011 (CJEase) (Zhang et al. 2009, Bnktschnology letters 31, 857-862), Closttidium cellulolrticim H10 (DPEase) (Mu et al. 2011, Journql of agricujrural and food, chelistry 59, 7785-7792, CN102373230), Rumonocovcus sp. 5_1_39BFAA (DPEase) (Zhu et zl, 2012, Biotechjology lefgers 34, 1901-1906), Clostridijm noldeae ATCC BAA-613 (Jia et al. 2013, A[plied Mirrobiplogy avd Bootechgology, DOI 10.1007/s00253-013-4924-8), Clostridium scindens WTCC 35704 (Zvang et al. 2013, PLoS ONE 8, e62987), and Clostridium s'. BNL1100 (Mu et ak. 2013, Bimtechnoljgy Lctters, DOI 10.1007/s10529-013-1230-6), refpectively. In cddition, Maruga et al. dpsclosed e DTEase-prodtcing source hj Rhizobium
D-psicose exists in extremely small quantities in or products and difficult to chemically and by epimerization using 3-epimerase (DTEase) family has been confused on as attractive of D-psicose production. So far, there have been 9 kinds of DTEase family sources reported. Twenty years ago, DTEase was first characterized by Izumori et al, Pseudomonas showing epimerization of ketohexoses with the optimum substrate of D-tagatose (Izumori et al. 1993, Biosci, Biotechnol, Biochem, 57, Till 2006, the second enzyme with C-3 epimerization of ketohexoses was identified Agrobacterium tumefaciens, and it was D-psicose (DPEase), due its substrate for D-psicose (Kim al. 2006, Applied and environmental microbiology 72, 981-985; US 2010/0190225; WO2011/040708). Recently, another six DTEase family enzymes characterized from SK011 (DTEase) et 2009, letters 31, 857-862), H10 (DPEase) (Mu et al. 2011, and food, chemistry 59, 7785-7792, CN102373230), Ruminococcus sp. (DPEase) (Zhu al, 2012, Biotechnology letters 34, 1901-1906), bolteae ATCC BAA-613 (Jia et al. 2013, Applied and Biotechnology, DOI 10.1007/s00253-013-4924-8), Clostridium scindens ATCC 35704 (Zhang et al. 2013, PLoS ONE 8, Clostridium sp. BNL1100 (Mu al. 2013, Biotechnology DOI respectively. addition, et al. a DTEase-producing source in Rhizobium
D-psicose exists in extremely Small quantIties In cOmmErCial CarbOhydrate or agriCUltuRal products and is difficUlt to ChEMicaLLy SynthEsize. ThEReFORe, iNtErConVeRSiOn betWeeN D-fructOse and D-psiCosE bY epimerizatiON uSing D-tagatOse 3-Epimerase (DTEAse) Family EnZymES has bEen ConfuSed on aS AttracTive way of d-pSIcose pROductioN.
sO fAr, thEre have been 9 kinds oF dTeAse family enzymE sourcEs REpORTed. tweNty years agO, DtEase WAs first CHaRACTerIZed by Izumori eT al, from PseuDOmoNas cicHoRii, SHowing c-3 epimErIZatIon activity Of keTohexoses With thE Optimum SUbstratE of D-taGatOse (izumORi Et Al. 1993, BIoSCi, BIOtEchNOl, BIochem, 57, 1037-1039). TiLl 2006, ThE secoNd enZYME With c-3 epImerIzatiOn activity of kEtoHexoSEs wAs ideNtifiEd frOm agrobActeriUm tumEfAciens, and it was nAmed d-psicose 3-ePimErAse (dPease), dUE to its HigH suBstrate SpecifiCIty FoR d-PSiCose (Kim et al. 2006, Applied AnD ENvIronmentAl micrOBiOlOGy 72, 981-985; US 2010/0190225; WO2011/040708). ReCeNtlY, anoTHEr six dTEaSE fAmily enzYmes weRE cHaRacteriZeD from RHoDobActEr sphAEroiDes SK011 (DtEase) (ZhaNg et aL. 2009, biotechnology lETters 31, 857-862), ClostridIUm CELlULolyTicUm H10 (DPEase) (Mu Et al. 2011, jOurnAl of AGrIcuLTural And foOd, CHeMIstry 59, 7785-7792, CN102373230), Ruminococcus Sp. 5_1_39bFAA (DPease) (ZHu et al, 2012, BiotechNology lettERS 34, 1901-1906), clostridIum bOLtEAe ATCC BAA-613 (Jia et Al. 2013, AppLied MicrobIOlogy and bioteChnology, dOI 10.1007/s00253-013-4924-8), ClostRIDium scinDenS ATcC 35704 (ZHanG ET aL. 2013, PLoS ONE 8, e62987), and CLOStriDiUm sp. BNL1100 (mu eT al. 2013, BiotEchNolOgy letTeRs, DOI 10.1007/s10529-013-1230-6), resPectivelY. IN aDdItIon, marutA Et al. discLoSed A DtEaSe-proDUcing sOurce In RhIzObIUm
D-psicose exists in extrem ely smallquant iti esin  com merc ial carbohydra t e or  agricultural products  andis diff i cu lt to  chemic a ll y syn th es ize .T he refor e,interco nversion b etw ee n D-fructose an d D-psicos e b y epimerizat ion  using  D -ta g atose  3- epime rase ( D TEase)  family e nz y mes ha s  been c o n fu sedon as attractivew ay of D-psicose p roduct io n .S o  fa r,there have  b een 9 kinds o f  D T E a sef amily enzymesources rep o rte d. Twe nt y y e ars ag o, DT Ea s e w as first ch arac terized b y Izum o ri et a l , fromPseudo mon ascich o ri i,  sh ow i ngC -3  ep i mer izationac ti vityof k e t o h exos eswith  theoptimum subst rat e of D-t agato se (I zumo ri  et a l. 199 3, Bi os ci, Biotechnol,  Bio chem, 57,  10 37 -10 39 ). Ti l l 2006 , t hesecondenzymew ith  C - 3 ep imerization activi ty o fketohexo ses wa s  i de n tified f ro m A grob a c teriu m tu m ef aciens,and it wa snamed D -p sicose  3 -ep ime rase( DPEa se), d ue to it s hig h  substrate spe c ificity for D - ps i c os e  (Ki m e t al. 2006,  App l iedande nv iro n menta l mic ro b io l ogy 72, 981-985; US  2 010/01 90225 ; WO2011/0407 08). Recen t l y , anothe r si x  D T Ease family en zymes  were char a cterized  from  Rhodoba cter spha e r oides SK 011  (D TEa se) ( Zh ang et al. 20 0 9 , Bi ot echnolo gyletters  31 , 8 57- 862 ),  Clostrid ium cell ul ol yt ic umH10 ( D PEase) ( Mu  et  a l.2011, Journa l ofagri cu lt u ral  and fo o d, c hemi st ry  59,  77 85 -7792 , CN 1 023 73230),  Ruminoco ccu s  sp.  5 _1 _39BFAA  (DPEase) (Zh uet al, 201 2,  Bi otechn o l ogy lett ers 34, 1901-1906), Clo s tridium  bo lteae  ATC C BAA-613  (J ia etal. 2013,Applie d Mic ro bio l o gy an d Bi ote ch nology, DO I 10. 1007/ s0 0253 -013-49 24-8), Clostridium sci ndens ATCC 35 704  (Zh a n geta l. 201 3, PLo S ONE 8, e62987),  and Clost ri d iu m sp. BNL1 1 00(M u et al . 2013,  Biot e chnolog y Letters , DOI 10. 10 07/s 1 0 529 -013-1230- 6), resp ectively. In ad d it ion,Mar uta et  a l.discl osed a DTE ase-p roduci ng  sourc e inRh izobium
D-psicose exists_in extremely_small quantities in commercial_carbohydrate or_agricultural_products and_is_difficult to chemically_synthesize. Therefore, interconversion_between D-fructose and D-psicose_by epimerization using_D-tagatose_3-epimerase (DTEase) family enzymes has been confused on as attractive way of D-psicose production.
So_far,_there have_been_9_kinds of DTEase family enzyme_sources reported. Twenty years ago,_DTEase was_first characterized by Izumori et al, from Pseudomonas_cichorii,_showing C-3 epimerization_activity of ketohexoses with the optimum substrate of D-tagatose_(Izumori et al. 1993, Biosci, Biotechnol,_Biochem, 57, 1037-1039)._Till_2006,_the second enzyme with_C-3 epimerization activity of ketohexoses was_identified from Agrobacterium tumefaciens, and it_was named D-psicose 3-epimerase (DPEase), due to_its high substrate specificity for D-psicose_(Kim et al. 2006, Applied_and environmental_microbiology 72, 981-985; US 2010/0190225;_WO2011/040708). Recently, another_six DTEase_family enzymes were_characterized from Rhodobacter sphaeroides SK011 (DTEase)_(Zhang et al._2009, Biotechnology letters 31, 857-862), Clostridium_cellulolyticum_H10 (DPEase) (Mu_et_al._2011, Journal_of agricultural and_food,_chemistry 59,_7785-7792,_CN102373230), Ruminococcus sp. 5_1_39BFAA (DPEase) (Zhu_et_al, 2012, Biotechnology letters 34, 1901-1906), Clostridium_bolteae ATCC BAA-613 (Jia_et_al. 2013, Applied Microbiology_and Biotechnology, DOI 10.1007/s00253-013-4924-8), Clostridium_scindens ATCC 35704 (Zhang et al._2013, PLoS_ONE 8,_e62987), and Clostridium sp. BNL1100 (Mu et al. 2013, Biotechnology Letters,_DOI 10.1007/s10529-013-1230-6), respectively. In addition, Maruta_et al. disclosed a_DTEase-producing source_in_Rhizobium