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
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3.2.1.23
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lacz
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adenovirus
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lysosomal
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lactose
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endothelial
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oligosaccharide
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artery
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phage
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adenovirus-mediated
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beta-glucosidase
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immunoassay
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retroviral
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beta-glucuronidase
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herpes
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lambda
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simplex
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luciferase
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cytomegalovirus
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neuraminidase
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viruses
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hydrolases
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bacteriophage
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glycosidases
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gm1
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liposome
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ganglioside
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p16ink4a
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alpha-galactosidase
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alpha-mannosidase
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osteogenic
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vaccinia
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adeno-associated
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replication-defective
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n-acetyl-beta-glucosaminidase
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runx2
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sialidase
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alpha-glucosidase
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sialic
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galactosylation
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plaque-forming
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osteoblast
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kluyveromyces
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telomerase
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analysis
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degradation
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diagnostics
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lysogens
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beta-hexosaminidase
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keratan
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vector-mediated
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biotechnology
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molecular biology
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synthesis
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environmental protection
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ganciclovir
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nutrition
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transglycosylation
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medicine
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industry
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nonviral
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food industry
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biofuel production
- 3.2.1.23
- lacz
- adenovirus
- lysosomal
- lactose
- endothelial
- oligosaccharide
- artery
- phage
-
adenovirus-mediated
- beta-glucosidase
-
immunoassay
-
retroviral
- beta-glucuronidase
-
herpes
- lambda
- simplex
- luciferase
- cytomegalovirus
- neuraminidase
- viruses
- hydrolases
- bacteriophage
- glycosidases
- gm1
- liposome
- ganglioside
- p16ink4a
- alpha-galactosidase
- alpha-mannosidase
-
osteogenic
- vaccinia
-
adeno-associated
-
replication-defective
- n-acetyl-beta-glucosaminidase
- runx2
- sialidase
- alpha-glucosidase
-
sialic
-
galactosylation
-
plaque-forming
-
osteoblast
- kluyveromyces
- telomerase
- analysis
- degradation
- diagnostics
-
lysogens
- beta-hexosaminidase
- keratan
-
vector-mediated
- biotechnology
- molecular biology
- synthesis
- environmental protection
- ganciclovir
- nutrition
-
transglycosylation
- medicine
- industry
-
nonviral
- food industry
- biofuel production
Reaction
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
3.2.1.23 beta-galactosidaseAdvanced search results
results (
results (Temperature Stability
Temperature Stability on EC 3.2.1.23 - beta-galactosidase
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TEMPERATURE STABILITY 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
0 - 25
60% of the maximum activity of the enzyme is determined at 25°C and 15% of the maximum activity is detected at 0°C, the enzyme is active in the range of temperature 4-8°C
0 - 35
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the enzyme remains stable from 0-35°C, above 35°C there is a constant drop of activity with about 60% relative activity at 40°C, 30% relative activity at 45°C, and no activity at 60-70°C
10 - 40
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stable for 100 hours at and below 10°C. At temperatures at and above 40°C enzyme is inactivated within 10 min
100
20 - 45
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ZD410 is stable up to 30°C and has only 17% of its activity at 45°C. It is completely inactivated at 50°C
20 - 50
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relatively stable between 20 and 50°C, the enzyme maintains 85% of its activity at 20-30°C and 70% at 50°C
25
30
35
37
37 - 75
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soluble bet-Gal is completely inactivated when it is pre-incubated at 75°C, whereas encapsulated bet-Gal retains above 90% of its maximum activity, even after being reused, preincubation at 37°C does not affect the enzymatic activity
40
40 - 60
40 - 65
the wild-type beta-galactosidase is fully stable at 40°C and 45°C for 16 h, respectively. At temperatures of 50, 55, 60 and 65°C wild type enzyme half-lives are 6, 3, 1.5 and 0.4 h respectively. Above 65°C occurs rapid inactivation with or without divalent ions
42
45
45 - 50
an enzyme stability assay reveals that the activity of GalA is significantly decreased when it is incubated at 45°C for 2 h, and all its activity is lost when it is incubated at 50°C
47
48
50
52
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half-life of beta-D-galactoside galactohydrolase pH 4.2 is 28 min, half-life of the beta-D-galactoside galactohydrolase pH 4.5 is 45 min
55
58
60
60 - 70
no activity is lost after incubation at 60°C for 60 min and more than 60% of the initial activity is retained after incubation at 70°C for 60 min, most of the enzymatic activity is lost within 2 min at 80°C
60 - 80
a sharp drop of activity occurs above 60°C, no activity is detected at 80°C
60 - 90
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kinetic modelling of the thermal and pH inactivation of the free and an immobilized form of the enzyme, inactivation mechanism, detailed overview
65
65 - 75
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the half-lives of the enzyme at 65°C, 70°C, 75°C, and 80°C are 128, 48, 17, and 2 h respectively
70
75
80
85
90
95
additional information
100
the mutant enzyme YG6762 shows 40% remaining activity after 1 h, and 30% remaining activity after 2 h, wild-type enzyme YH4502 shows over 75% remaining actiivty after 1 h, and more than 50% remiaing activity after 2 h
100
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purified enzyme, pH 6.5, complete loss of activity after 15 min
30
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BgaS, mutant BgaS7, and mutant BgaS6 loose all detectable activity after 75, 90, and 120 min, respectively
30
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1 h, pH 4.0-9.0, stable, more than 60% loss of activity after 10 min at pH 3.5
30
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30 min, recombinant hybrid enzyme, stable, the wild-type enzyme loses 45% activity within 60 min
40
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15 min, recombinant hybrid enzyme, stable, the wild-type enzyme loses 10% activity within 10 min
40
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about 30% loss of activity after 5 h, about 75% loss of activity after 33 h
40 - 60
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when the temperature is higher than 60°C for immobilized enzyme (on Ca-alginate gel beads) and above 50°C for free enzyme, an obvious loss of activity is observed, below 40°C the activity for both forms of enzymes decreases substantially
40 - 60
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the enzyme retains 86.26% of its activity when kept for 10 min at 40°C however it loses 90.85% of its activity at 50°C and 94.89% at 60°C
42
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80 min,75% loss of leukocte enzyme from GM1 gangliosidosis heterozygotes,70% loss of fibroblast enzyme from GM1 gangliosidosis heterozygotes
45
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50 min, about 50% loss of phlorizin hydrolase activity, about 70% loss of lactase activity
45
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about 60% loss of activity after 5 h, about 90% loss of activity after 25 h
50
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half-life of immobilized enzyme from strain 11-1O at pH 6.5 when lactose solution is passed through the column is 42 days, when bovine milk is passed through the column the half-life is 32 days
50
5 min, rapid inactivation, purified recombinant enzyme
50
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15 min, recombinant hybrid enzyme, loss of 40% activity, the wild-type enzyme loses 60% activity
50
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about 90% loss of activity after 2 hm complete inactivation agter 5 h
50
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56% loss of activity after 3 min, 36% loss of activity in presence of 20 mM MgCl2
50
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55% loss of activity after 4 min, 83% loss of activity after 10 min, 33% loss of activity after 4 min in presence of 10 mM MgCl2, 52% loss of activity after 10 min in presence of 10 mM MgCl2
50
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half-life of immobilized enzyme in a continuous stirred reactor: 50 days
50
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half-life 8 h for native enzyme, 27 h for immobilized enzyme, respectively
55
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40 min, in presence of 0.1 M mercaptoethanol and 0.01 MgCl2, 50% loss of activity. Without mercaptoethanol complete loss of activity after 10 min
55
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half-life of immobilized enzyme in a continuous stirred reactor: 15 days
55
10 min, complete and irreversible inactivation after 10 min
55
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5 min, loss of 42% activity in 0.5 M K2HPO4 buffer, no activity loss in 1.5 M K2HP04
55
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30 min, 70% loss of activity, 42% loss of activity in presence of 2 mg/ml bovine serum albumin
60
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10 min, 88% remaining activity of the mutant enzyme, 21% of the wild-type enzyme
60
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entrapped cross-linked enzyme in complex with concanavalin A: 49% remaining activity after 6 h, free enzyme: 3% remaining activity after 5 h
60
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10 min, more than 60% loss of activity, 18% loss of activity in presence of 4 mg/ml bovine serum albumin
60
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pH 7.2, 4 h, in presence of 1.75 M lactose and 0.01 mM MnCl2, stable up to
65
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the half-lives are 128 min and 118 min for purified isozymes BGT I and BGT II, respectively
65
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t1/2: 14.5 for enzyme immobilized on calcium alginate, 2 h for free enzyme
70
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3 h, in presence of 2-mercaptoethanol, enzyme from transformant and from strain NA10, stable
70
Caldariella acidophila
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half-life: 550 h, half life of the enzyme in whole cells entrapped in a polyacrylamide gel in presence of lactose: 28 days
70
1 h, the native enzyme retains 67% of its activity while the recombinant enzyme preserves 35%
70
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half-life: 720 h, thermal deactivation of galactooligosaccharide production
75
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10 min, 32% remaining activity of the mutant enzyme, inactivation of the wild-type enzyme
75
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3 h, in presence of 2-mercaptoethanol, enzyme from transformant is stable, enzyme form strain NA10 loses 29% of its activity
75
half-life of mutant enzyme F441Y is 75 h, half-life of mutant enzyme F359Q is 85 h. Activity of wild-type enzyme increases slowly within the first 45 h, it retains 90% of its initial activity after incubation for approximately 80 h. After 80 h, the activity decreases rapidly
75
50% loss of activity after 12 h, recombinant mutant enzyme F441Y
75
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half-life: 208 h, thermal deactivation of galactooligosaccharide production
80
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entrapped cross-linked enzyme in complex with concanavalin A: 63% remaining activity, free enzyme: 2% remaining activity
80
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3 h, 37% loss of activity of transformant enzyme, 95% loss of activity of enzyme form strain NA10
80
Kerstingiella geocarpa
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1 h, complete inactivation. 47% of the activity regenerates within 6 h at 25°C
80
50% loss of activity after 11 h, recombinant mutant enzyme F441Y
80
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half-life: 77 h, thermal deactivation of galactooligosaccharide production
85
50% loss of activity after 5.5 h, recombinant mutant enzyme F441Y
85
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half-life: 42 h, thermal deactivation of galactooligosaccharide production
90
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10 min, 10% remaining activity of the mutant enzyme, inactivation of the wild-type enzyme
90
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half-life: 9.3 h, thermal deactivation of galactooligosaccharide production
95
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purified enzyme, pH 6.5, complete loss of activity after 120 min
additional information
temperature stability profile of the recombinant enzyme, overview
additional information
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temperature stability profile of the recombinant enzyme, overview
additional information
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thermostability of recombinant wild-type and mutant enzymes, overview
additional information
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thermostability of soluble and immobilized enzymes at enzyme concentration 0.1-15 mg/ml
additional information
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thermostability of soluble and immobilized enzymes at enzyme concentration 0.1-15 mg/ml
additional information
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enzyme becomes remarkably heat labile in the presence of fructose 1,6-diphosphate
additional information
Kerstingiella geocarpa
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galactose protects against irreversible thermoinactivation
additional information
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thermal deactivation is fit to a kinetic model
additional information
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thermal stability is improved in presence of MgCl2, strain L103
additional information
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thermal stability is improved in presence of MgCl2, strain L461
additional information
favorable thermostability within a broad range of pHs (6.09.0), its activity decreases below 10% for 15 min at 60°C without substrate protection
additional information
Saccharomyces fragilis
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thermostability of soluble and immobilized enzymes at enzyme concentration 0.1-15 mg/ml
