Purification and characterization of a thermostable α-glucosidase from aBacillus subtilis high-temperature growth transformant

1991 ◽  
Vol 22 (5) ◽  
pp. 273-278 ◽  
Author(s):  
Bradley M. Krohn ◽  
James A. Lindsay
Keyword(s):  
High Temperature ◽  
Purification And Characterization ◽  
Temperature Growth

High-temperature growth and spectroscopic characterization of Er,Yb:YAl3(BO3)4 epitaxial thin layers

2010 ◽  
Vol 32 (10) ◽  
pp. 1377-1379 ◽  
Author(s):  
N. Tolstik ◽  
S. Heinrich ◽  
A. Kahn ◽  
E. Volkova ◽  
V. Maltsev ◽  
...  
Keyword(s):  
High Temperature ◽  
Spectroscopic Characterization ◽  
Thin Layers ◽  
Temperature Growth

High-temperature growth and characterization of (Er,Yb):YAl3(BO3)4 and NdAl3(BO3)4 epitaxial layers

2014 ◽  
Vol 401 ◽  
pp. 547-549 ◽  
Author(s):  
E. Volkova ◽  
V. Maltsev ◽  
O. Kolganova ◽  
N.I. Leonyuk
Keyword(s):  
High Temperature ◽  
Epitaxial Layers ◽  
Temperature Growth

scholarly journals PURIFIKASI PARSIAL DAN KARAKTERISASI ß-GALAKTOSIDASE Lactobacillus plantarum B123 INDIGENOS DAN HIDROLISIS LAKTOSA UNTUK PRODUKSI SUSU ULTRA HIGH TEMPERATURE RENDAH LAKTOSA

2015 ◽  
Vol 17 (2) ◽  
pp. 147-161
Author(s):  
Tatik Khusniati ◽  
Neny Mariyani ◽  
Hanifah Nuryani Lioe ◽  
Didah Nur Faridah ◽  
Abdul Choliq ◽  
...  
Keyword(s):  
High Temperature ◽  
Lactobacillus Plantarum ◽  
Lactose Intolerance ◽  
Specific Activity ◽  
Partial Purification ◽  
Lactose Hydrolysis ◽  
Galactosidase Activity ◽  
Purification And Characterization ◽  
Uht Milk

β-Galactosidase is enzyme which hidrolyze lactose to glucose and galactose. This enzyme is used in production low lactose milk for consumption human which have lactose intolerance. Partial purification of β-galactosidase is important to be conducted to increase  β-galactosidase activity in order to its hydrolysis potency on UHT milk lactose increased.This research was aimed to production by partially purification and characterization indigenous β-galactosidase from Lactobacillus plantarum B123, and lactose hydrolysis for production low lactose UHT milk. Partially purification were precipitation following dialysis. Characterization included optimazion and stabilization of enzyme, while lactose hydrolisis for production low lactose UHT milk was detected by enzymatic GOD-POD kit. The results showed that production of β-galactosidase by using partial purification increased from 21.51 ± 0.23 U/mL (crude) to 106.34 ± 0.56 U/mL (dialysis).  The optimum crude β-galactosidase activity was reached in precipitation by using 60 % ammonium sulphate.  The purity of crude β-galactosidase increased 3.71 times after precipitation, and 14.28  times  after dialysis. Characterization of β-galactosidase showed that  optimum activities of crude and dialyzed β-galactosidase were at pH 6.5 and 50 oC, respectively. Stability of crude β-galactosidase incubated for 1 h were at pH: 5.0-8.5 and 25-50 °C. Specific activity of crude β-galactosidase was 15.05 U/mg protein, while that dialyzed β-galactosidase was 109.58 U/mg protein. Lactose hidrolysis to produce low lactose UHT milk showed that glucose concentration increased with the increase of hidrolysis time. Time needed to hidrolyze lactose 50 % with 4.8 U/mL β-galactosidase at 50°C was 6.08 h. In conclusion that indigenous β-galactosidase from Lactobacillus plantarum B123 purified partially can be used as lactose hidrolyzer in production of low lactose UHT milk.Key words : b-galactosidase, indigenous Lactobacillus plantarum B123, purification, lactose hidrolysis, UHT Milk

Purification and characterization of the heat-labile α-amylase secreted by the psychrophilic bacterium TAC 240B

1999 ◽  
Vol 45 (6) ◽  
pp. 452-457 ◽  
Author(s):  
Jean-Pierre Chessa ◽  
Georges Feller ◽  
Charles Gerday
Keyword(s):  
Molecular Structure ◽  
High Temperature ◽  
Low Temperature ◽  
Sea Water ◽  
Maximal Activity ◽  
Psychrophilic Bacterium ◽  
Purification And Characterization ◽  
Allosteric Effector ◽  
Psychrophilic Enzyme

A total of 59 bacteria samples from Antarctic sea water were collected and screened for their ability to produce α-amylase. The highest activity was recorded from an isolate identified as an Alteromonas species. The purified α-amylase shows a molecular mass of about 50 000 Da and a pI of 5.2. The enzyme is stable from pH 7.5 to 9 and has a maximal activity at pH 7.5. Compared with other α-amylases from mesophiles and thermophiles, the "cold enzyme" displays a higher activity at low temperature and a lower stability at high temperature. The psychrophilic α-amylase requires both Cl-and Ca2+for its amylolytic activity. Br-is also quite effecient as an allosteric effector. The comparison of the amino acid composition with those of other α-amylases from various organisms shows that the cold α-amylase has the lowest content in Arg and Pro residues. This could be involved in the principle used by the psychrophilic enzyme to adapt its molecular structure to the low temperature of the environment. Key words: α-amylase, psychrophilic microorganisms, Antarctic.

Purification and characterization of phosphoglucomutase from peas

1994 ◽  
Vol 92 (3) ◽  
pp. 479-486 ◽  
Author(s):  
Cynthia M. Galloway ◽  
W. Mack Dugger
Keyword(s):  
Purification And Characterization
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