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3.2.1.23: beta-galactosidase

This is an abbreviated version!
For detailed information about beta-galactosidase, go to the full flat file.

Word Map on EC 3.2.1.23

Reaction

beta-D-galactopyranosyl-(1-4)-beta-D-galactopyranosyl-(1-6)-beta-D-galactopyranosyl-(1-3)-beta-D-galactopyranose
+ 3 H2O = 4 beta-D-galactopyranose

Synonyms

Aabeta-gal, Acid beta-galactosidase, B-GAL, BbgI, BbgII, BbgIII, BbgIV, beta galactosidase, beta-D-galactohydrolase, beta-D-galactosidase, beta-D-galactoside galactohydrolase, beta-D-glactanase, beta-D-lactosidase, beta-gal, beta-Gal 1, beta-Gal 2, beta-Gal II, beta-galactosidase, beta-galactosidase I, beta-galactosidase II, beta-galactosidase III, beta-galactosidase IV, beta-galase, beta-lactosidase, betagal, betaGly4, betaGS, BGA, BgaB, BgaBM, bgaD, BgaH, BGAL, BGAL1, BGAL10, BGAL11, BGAL12, BGAL13, BGAL14, BGAL15, BGAL16, BGAL17, BGAL2, BGAL3, BGAL4, BGAL5, BGAL6, BGAL7, BGAL8, BGAL9, BgalA, BgAP, BgaS, BgaX, BGL1, BglAp, BGT I, BGT II, cold-active beta-galactosidase, CTP-beta-gal, driselase, EABase, endo-beta-galactosidase, Exo-(1-->4)-beta-D-galactanase, exo-beta-(1->3)-D-galactanase, Gal-2, Gal-5, GAL1, Gal2, Gal3, Gal4, GALA, galactanase, galactosidase, galactosidase, beta, GALB, gherkin lactase, H-BgaS, hcbetagal, Hlac_2868, Hydrolact, LacA, LACS, lactase, lactase phlorizin hydrolase, lactosylceramidase II, Lactozym, Lactozym 3000L, LPH, Maxilact, Maxilact-L/2000, MeBglD2, More, ONPGase, Oryzatym, p-nitrophenyl beta-galactosidase, PF1208, PRGH1, S 2107, SA-beta-GAL, SA-betagal, senescence-associated beta-galactosidase, SPD_0065 protein, SR12 protein, Ss beta-gal, SSO3019, SSU0587, Sumiklat, Trilactase, XC1214, XG-specific beta-galactosidase, YesZ, YH4502, ZD410

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.23 beta-galactosidase

General Stability

General Stability on EC 3.2.1.23 - beta-galactosidase

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
10% inactivation after 4 h in 40% tetraglyme, 20% inactivation after 4 h in 70% tetraglyme, 50% inactivation after 4 h in 80% tetraglyme
-
15% inactivation after 4 h in 40% triethyl phosphate, 45% inactivation after 4 h in 50% triethyl phosphate, 52% inactivation after 4 h in 60% triethyl phosphate, 67% inactivation after 4 h in 70% triethyl phosphate, 85% inactivation after 4 h in 80% triethyl phosphate
-
20% inactivation after 4 h in 40% triethyl phosphate, 42% inactivation after 4 h in 50% triethyl phosphate, 53% inactivation after 4 h in 60% triethyl phosphate, 64% inactivation after 4 h in 70% triethyl phosphate, 82% inactivation after 4 h in 80% triethyl phosphate
-
25% inactivation after 10 h in 0.8% Tween 80 in Tris-HCl buffer
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4 M urea, irreversible inactivation
-
5% inactivation after 4 h in 60% tetraglyme, 35% inactivation after 4 h in 80% tetraglyme
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50% inactivation after 10 h in 5% SDS in Tris-HCl buffer
-
87% inactivation after 10 h in 0.5% SDS in Tris-HCl buffer
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about 40% of the initial enzymatic activity is recovered after beta-Gal encapsulation in the silica matrix
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activity is irreversibly lost within min in low salt buffers, below 0.5 M
covalent immobilization, and additional stabilization of a thermophilic poly-His-tagged beta-galactosidase by using novel heterofunctional chelate-epoxy Sepabeads
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dilute purified BGAL preparation with a protein concentration less than 0.1 mg/ml is unstable with a t1/2 of about 13 h at 4°C and pH 5.0, at a protein concentration of 0.1 mg/ml the enzyme has a t1/2 of about 10 days at 4°C and pH 5.0
-
dissociation and partial unfolding of the dimeric enzyme under high hydrostatic pressure, more resistant in presence of polyols
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enzyme immobilized by DEAE-cellulose and calcium alginate allows a 47% and 70% lactose hydrolysis, respectively, to be achieved within 48 h after repeated use for twenty times
-
kinetic modelling of the thermal and pH inactivation
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lactose provides a heat-protective effect
-
loss of activity on freezing
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Mg2+ is required for enzyme stability
non-specific enzyme stabilization by amino acids, overview
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polyaniline chitosan nanocomposite-bound and polyaniline chitosan silver nanocomposite-bound enzymes are more resistant to the exposure caused by the higher concentration of added D-glucose, D-galactose, and vitamin C
-
the enzyme immobilized on Sepharose is more stable
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the enzyme is more stable at 5 mM phosphate than at 50 mM phosphate Ca2+ destabilizes lactose and 2-mercaptoethanol stabilize
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the enzyme is strongly resistant to pepsin and trypsin digestion, after incubation in SGF at 37°C for 60 min recombinant BgalA retains almost all of its activity at the whole stomach stage with or without the presence of pepsin
the enzyme remains highly stable in solution or immobilized at room temperature in the absence of protein stabilizers, the His tag does not affect activity
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the immobilized enzyme (on Ca-alginate gel beads) loses about 80% of activity after the initial cycle in all cases, the activity decreases gradually in the ensuing cycles, and the residual activity is only around 15% after 3 cycles
-
the purified enzyme retains 68% residual activity after in vitro exposure to simulated gastric conditions (pepsin at pH 2.0) for 2 h
the unpurified beta-galactosidase displays a high level of stability when exposed to simulated intestinal conditions in vitro for 4 h
the unpurified enzyme displays a high level of stability when exposed to simulated intestinal conditions in vitro for 4 h
thermostability is enhanced by CaCl2
-
unstable in 0.2 M urea
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when the recombinant enzyme from active inclusion bodies is utilized for lactose conversion in a repetitive batch mode, more than 54% (90°C) or 88% (10°C) of the original enzyme activity is retained after 10 conversion cycles under optimum conditions