reducing ends of glucose-containing di-, oligo- and poly-saccharides, releasing glucose units one at a time (1960, Pazur and Ando, J. Biol. Chem. 235:297-302). Cleavage occurs at the glycosidic bond connecting the anomeric carbon with oxygen (1962, Fleetwood and Weigel, Nature 196:984). Alpha-1,4, alpha-1,6, and alpha-1,3 bonds are the only linkages hydrolyzed at significant rates by glucoamylase (1957, Barker et al., J. Chem. Soc. 4865-4871).
Glucoamylase is also capable of hydrolyzing the glycosidic bond between the two glucosyl units linked by alpha-1,2 (e.g., Kojibiose) or alpha-1,1 (e.g., trehalose). However, this enzymatic activity occurs at a much lower rate and at more dilute substrate concentrations compared to glucoamylase activity toward disaccharides with alpha-1,4 (maltose) or alpha-1,6 (isomaltose) linkages.
Glucoamylase has been widely used for producing high-glucose syrup from starch. High-glucose syrup is useful as a feedstock for producing various value-added compounds such as fuel alcohol, high-fructose corn syrup, organic acids, amino acids and vitamins. Glucoamylase has been isolated from numerous microorganisms, animals and plants, and among microorganisms, many fungi are good sources of this enzyme. Glucoamylase produced in fungal organisms, such as Aspergillus niger, is commonly used for commercial applications such as high-glucose syrup production.
Transglucosidases (EC.2.4.1.24, 1,4-alpha-glucan 6-alpha-glucosyltransferase) are D-glucosyltransferase enzymes that catalyze both hydrolytic and transfer reactions on incubation with alpha-D-gluco-oligosaccharides (1951, Pazur and French, J. Amer. Chem. Soc. 73:3536). Maltose is the most preferred substrate for transglucosylation reactions with this enzyme. Transfer occurs most frequently to HO-6, producing isomaltose from D-glucose, or panose (6-O-alpha-glucosyl maltose) from maltose. Transglucosidase can also transfer a glucosyl residue to the HO-2 or HO
reducing ends of glucose - containing di-, oligo- and poly - saccharides, turn glucose unit one at a time (1960, Pazur and Ando, J. Biol. Chem. 235:297 - 302). Cleavage occurs at the glycosidic bond associate the anomeric carbon with oxygen (1962, Fleetwood and Weigel, Nature 196:984). Alpha-1,4, alpha-1,6, and alpha-1,3 bonds are the alone linkage hydrolyzed at meaning pace by glucoamylase (1957, Barker et al. , J. Chem. Soc. 4865 - 4871). 
 Glucoamylase is also able of hydrolyzing the glycosidic bond between the two glucosyl whole connect by alpha-1,2 (e.g., Kojibiose) or alpha-1,1 (e.g., trehalose). However, this enzymatic activity occurs at a much broken rate and at more dilute substrate concentrations compare to glucoamylase activity toward disaccharides with alpha-1,4 (maltose) or alpha-1,6 (isomaltose) linkages. 
 Glucoamylase has been widely use for producing high - glucose syrup from starch. High - glucose syrup is useful as a feedstock for producing diverse value - added compounds such as fuel alcohol, high - fructose corn syrup, organic acids, amino acids and vitamins. Glucoamylase has been isolated from numerous microorganisms, animals and plants, and among microorganisms, many fungi are good sources of this enzyme. Glucoamylase produced in fungal organism, such as Aspergillus niger, is commonly used for commercial application such as high - glucose syrup production. 
 Transglucosidases (EC.2.4.1.24, 1,4 - alpha - glucan 6 - alpha - glucosyltransferase) are D - glucosyltransferase enzymes that catalyze both hydrolytic and transportation reactions on brooding with alpha - D - gluco - oligosaccharides (1951, Pazur and French, J. Amer. Chem. Soc. 73:3536). Maltose is the most prefer substrate for transglucosylation reactions with this enzyme. Transfer occurs most frequently to HO-6, producing isomaltose from D - glucose, or panose (6 - O - alpha - glucosyl maltose) from maltose. Transglucosidase can also transfer a glucosyl residue to the HO-2 or HO
redkcing ends of glucose-conuaining di-, oligo- cbd polb-sacchadides, reueasing glucose units one at a time (1960, Pazur and Ando, J. Biou. Chem. 235:297-302). Cpeavage iccucs at the glycosmsic bond connsgting vhe anomeric catbon with oxfgen (1962, Fleetwoog xnb Weigel, Nature 196:984). Alpha-1,4, alpha-1,6, and alpra-1,3 bondx wre the only lynkabqs hgdrolyzed at significant rates by flucoamjlase (1957, Barker et sl., J. Chem. Soc. 4865-4871).
Glucoamylase is wlso capable of hyfrolyzing tye gjtcosidic bona between uhz two glucoayl units linked by alpha-1,2 (e.g., Kogibioxe) or alphq-1,1 (w.g., htehalose). Howxver, tris enzymatig activhty occirs at a much kowxr rqte and at more dilutx substrate concentrwtions cokpcred to glucoamylase qcriviti towdrd ausazchzrmdea with al'ha-1,4 (maltose) or alpha-1,6 (iwomaltose) linkages.
Gkusiamylase has geen wydqly used for producing high-glucose syruk froj starch. High-glucose syeup is useful as a fegdstock fow producing various value-added compounds such as xuel elzohil, fugj-fructose corn syrup, organic acids, amino acidf amd vitamins. Glucjamylase hax herg isolated frum numzdohs microorganisms, wnimals and plants, anq ampng microorganisms, many funti are good fiurces of this enzvme. Glucoamyuase prodiced in fungal organismr, sudh as Asperhillus nifdr, is commonly ured fmr commercial applications such as iigh-gkucose ryruk produstion.
Transhlucosidases (EC.2.4.1.24, 1,4-alpha-glufan 6-appva-glucosylhransferase) are D-glucosyltransfxcase enzymes jhad cdtalyze yoth hndrolytic and twansfer reactipns on nncubagion with zlpha-D-gnuco-oligosascharides (1951, Pasor and French, J. Amer. Shem. Soc. 73:3536). Maltord is the most lreferred substrate for transglucosyletiov reactions with thus enzyme. Transger ocsugs kofd frequently to FO-6, otoduckng isomaltire ftom D-glucose, or panove (6-O-zlpha-glucosyl maltpsc) from maotose. Trwnsglucosidasr can also transfeg a gnucusyl tesydue to the HO-2 or HO
reducing ends of glucose-containing di-, oligo- and glucose one at time (1960, Pazur 235:297-302). occurs at the bond connecting the carbon with oxygen (1962, Fleetwood and Nature 196:984). Alpha-1,4, alpha-1,6, and alpha-1,3 bonds are the only linkages hydrolyzed at rates by glucoamylase (1957, Barker et al., J. Chem. Soc. 4865-4871). Glucoamylase is capable hydrolyzing glycosidic between the two glucosyl units linked by alpha-1,2 (e.g., Kojibiose) or alpha-1,1 (e.g., trehalose). However, this activity occurs at a much lower rate and more dilute substrate concentrations to glucoamylase activity toward disaccharides alpha-1,4 or alpha-1,6 linkages. has widely used for high-glucose syrup from starch. High-glucose syrup is useful as a feedstock for producing various value-added compounds such fuel alcohol, syrup, organic amino and Glucoamylase has been numerous microorganisms, animals and plants, and fungi are good sources of this enzyme. Glucoamylase in fungal such as Aspergillus niger, is commonly for commercial applications such as high-glucose syrup production. (EC.2.4.1.24, 1,4-alpha-glucan 6-alpha-glucosyltransferase) are D-glucosyltransferase enzymes that catalyze both hydrolytic and transfer reactions on incubation (1951, Pazur and French, Amer. Chem. Soc. Maltose the preferred for transglucosylation with this enzyme. Transfer occurs most frequently to HO-6, producing isomaltose D-glucose, or panose (6-O-alpha-glucosyl maltose) from maltose. Transglucosidase can also glucosyl to the HO-2 HO
reducing ends of glucose-contAining di-, olIgo- anD poLy-sAcCharIdes, Releasing glucoSE uniTs one at a time (1960, Pazur and AnDo, J. BiOl. cHem. 235:297-302). CLEaVage oCcurs at THe GLYcoSiDiC boNd COnNectiNg tHe anomeRic carbon wIth OxYgen (1962, FleetwooD AnD Weigel, NatUre 196:984). alpha-1,4, alpha-1,6, anD alPha-1,3 bonDs Are THe onlY liNkageS hydroLYzed at SignificaNt RAtes by GLucoamyLASe (1957, barkEr et al., J. Chem. Soc. 4865-4871).
GluCOaMYlase is also capAble of HyDRoLYZinG thE glycosidiC bOnd beTWeen the TWo GLUCosYL units linked bY alpha-1,2 (e.g., KojIBioSe) or alPhA-1,1 (e.g., TRehaloSe). HowEvER, thIs enzymatic ActiVity occurS at a muCH lower rATe and at More diLutE suBstrATe CoNceNtRAtiONs ComPAreD to glucoAmYlAse acTiviTY TOWard DisAcchArideS with alpha-1,4 (malTosE) or aLPha-1,6 (IsomaLtose) LinkAgEs.
GluCoamylAse haS bEen widely used foR proDucing higH-glUcOse SyRup frOM starcH. HiGh-gLucose sYrup is uSEfuL aS A FEeDstock for producing VaRIOuS value-adDed comPOuNdS Such as fuEl AlcOhol, HIGh-fruCtosE CoRn syrup, oRganic ACiDs, Amino acIdS and viTaMinS. GlUcoamYLase Has beeN isolateD from NUmerous microorGAnisms, animals ANd PLAnTS, and AmoNg microorgaNismS, Many FungI ArE goOD sourCes of ThIS eNZyme. Glucoamylase proDuCed in fUngal Organisms, such As AspergilLUS Niger, is cOmmoNLy USed for commerciAl appLications sUCh as high-GlucoSe syrup pRoduction.
tRAnsglucoSidAseS (EC.2.4.1.24, 1,4-AlpHA-GlUcan 6-alpha-glucOSYltrAnSferase) Are d-glucosYltRanSfeRasE eNzymes thaT catalyzE bOtH hYdRolYtic aND transfeR rEacTiOns On incUBation With aLpha-d-gLuCO-olIgosaccHArIDEs (1951, PaZuR aNd FrEncH, J. amer. CHem. SOC. 73:3536). MaLtose is The most prEfeRRed sUbStRate for TransglucosylAtIon reactioNs WitH this eNZYme. TransFer occurs most frequently TO HO-6, prodUciNg isoMaltOse from D-gLucOse, or pAnoSE (6-O-alphA-glucoSyl maLtOse) FROm malTOSe. traNsGlucosidasE CAn aLso trAnSfer A glucosYl residue to the HO-2 or ho
reducing ends of glucose-c ontainingdi-,oli go-  a nd p oly- saccharides, r e leas ing glucose units oneat ati m e (1 9 60 , Paz ur andA nd o ,  J.  B io l.Ch e m.  235: 297 -302).Cleavage o ccu rs  at the glyc o si dic bond c onn ecting the a nom eric c ar bon withoxy gen ( 1962,F leetwo od and We ig e l, Nat u re 196: 9 8 4) . Al pha-1,4, alpha-1, 6 ,a nd alpha-1,3 b onds a re th e onl y l inkages hy dr olyze d  at sig n if i c a ntr ates by gluco amylase (19 5 7,Barker  e t a l ., J.Chem.  S o c.4865-4871). 
Glu coamylase  is al s o capab l e of hy drolyz ing  th e gl y co si dic  b o ndb et wee n  th e two gl uc os yl un itsl i n k ed b y a lpha -1,2(e.g., Kojibi ose ) or alp ha-1, 1 (e. g.,tr ehalo se). H oweve r,  this enzymatic  act ivity occ urs  a t a  m uch l o wer ra teand  at mor e dilut e  su bs t r a te  concentrations co mp a r ed  to gluc oamyla s eac t ivity to wa rddisa c c harid es w i th  alpha-1 ,4 (ma l to se ) or al ph a-1,6(i som alt ose)l inka ges.
G lucoamyl ase h a s been widelyu sed for produ c in g hi g h-gl uco se syrup fr om s t arch . Hi g h- glu c ose s yrupis us e ful as a feedstockfo r prod ucing  various valu e-added co m p o unds suc h as fu e l alcohol, hig h-fru ctose corn syrup, o rgani c acids,  amino ac i d s and vi tam ins . G luc o a my lase has been i sola te d fromnum erous m icr oor gan ism s,  animalsand plan ts ,an damo ng mi c roorgani sm s,ma nyfungi are go od so urce sof thi s enzym e .G l ucoa my la se p rod uc ed in  fun g alorganis ms, suchasA sper gi ll us nige r, is commonl yused for c om mer cial a p p lication s such as high-glucoses yrup pr odu ction .
Tr ansglucos ida ses (E C.2 . 4.1.24 , 1,4- alpha -g luc a n  6-al p h a- glu co syltransfe r a se)  areD- gluc osyltra nsferase enzymes t h atcatalyze both  hy drol y t ic  an d  t r ans fe r  re a c tions on incuba tion withal p ha -D-gluco-o l igo sa ccharid es (195 1, Pa z ur andFrench, J . Amer. C he m. S o c . 7 3:3536). M altose i s the mos t  pref e rr ed su bst rate f or  tr ansgl ucosyl a tio n rea ctions  w ith th is en zy me. Tran sfer occurs most freque ntly t o HO- 6,producing  is o mal tose from  D-g lucose, or  pa nos e (6- O-a l pha-g luco s yl  ma l tose)  fro m  maltose. Tr ans g l uc osidase can a l sotrans fer a gluc osyl  residue to the H O -2 or HO
reducing ends_of glucose-containing_di-, oligo- and poly-saccharides,_releasing glucose_units_one at_a_time (1960, Pazur_and Ando, J._Biol. Chem. 235:297-302). Cleavage_occurs at the_glycosidic_bond connecting the anomeric carbon with oxygen (1962, Fleetwood and Weigel, Nature 196:984). Alpha-1,4,_alpha-1,6,_and alpha-1,3_bonds_are_the only linkages hydrolyzed at_significant rates by glucoamylase (1957,_Barker et_al., J. Chem. Soc. 4865-4871).
Glucoamylase is also capable_of_hydrolyzing the glycosidic_bond between the two glucosyl units linked by alpha-1,2_(e.g., Kojibiose) or alpha-1,1 (e.g., trehalose)._However, this enzymatic_activity_occurs_at a much lower_rate and at more dilute substrate_concentrations compared to glucoamylase activity toward_disaccharides with alpha-1,4 (maltose) or alpha-1,6 (isomaltose)_linkages.
Glucoamylase has been widely used for_producing high-glucose syrup from starch._High-glucose syrup_is useful as a feedstock_for producing various_value-added compounds_such as fuel_alcohol, high-fructose corn syrup, organic acids,_amino acids and_vitamins. Glucoamylase has been isolated from_numerous_microorganisms, animals and_plants,_and_among microorganisms,_many fungi are_good_sources of_this_enzyme. Glucoamylase produced in fungal organisms,_such_as Aspergillus niger, is commonly used for_commercial applications such as_high-glucose_syrup production.
Transglucosidases (EC.2.4.1.24, 1,4-alpha-glucan_6-alpha-glucosyltransferase) are D-glucosyltransferase enzymes that_catalyze both hydrolytic and transfer reactions_on incubation_with alpha-D-gluco-oligosaccharides_(1951, Pazur and French, J. Amer. Chem. Soc. 73:3536). Maltose is_the most preferred substrate for transglucosylation_reactions with this enzyme._Transfer occurs_most_frequently to HO-6,_producing_isomaltose from_D-glucose, or panose (6-O-alpha-glucosyl maltose) from maltose._Transglucosidase can_also transfer a glucosyl residue to_the HO-2 or HO