Purification and characterization of endo-?-1,3-1,4-d-glucanase activity from Bacillus licheniformis

1988 ◽  
Vol 29 (1) ◽  
pp. 32-38 ◽  
Author(s):  
Jorge Lloberas ◽  
Enrique Querol ◽  
Jordi Bernu�s
2009 ◽  
Vol 42 (1) ◽  
pp. 63-68 ◽  
Author(s):  
Mário Lettieri Teixeira ◽  
Florencia Cladera-Olivera ◽  
Juliana dos Santos ◽  
Adriano Brandelli

2010 ◽  
Vol 89 (3) ◽  
pp. 645-654 ◽  
Author(s):  
Onladda Juajun ◽  
Thu-Ha Nguyen ◽  
Thomas Maischberger ◽  
Sanaullah Iqbal ◽  
Dietmar Haltrich ◽  
...  

2006 ◽  
Vol 129 (1-3) ◽  
pp. 289-302 ◽  
Author(s):  
Valquiria B. Damiano ◽  
Richard Ward ◽  
Eleni Gomes ◽  
Heloiza Ferreira Alves-Prado ◽  
Roberto DA Silva

2010 ◽  
Vol 86 (6) ◽  
pp. 1867-1875 ◽  
Author(s):  
Yoichi Toyokawa ◽  
Hiroaki Takahara ◽  
Alissara Reungsang ◽  
Masakazu Fukuta ◽  
Yuki Hachimine ◽  
...  

1986 ◽  
Vol 64 (9) ◽  
pp. 914-922 ◽  
Author(s):  
Anthony G. Day ◽  
Stephen G. Withers

The β-glucosidase from Alcaligenes faecalis has been purified to homogeneity (880-fold purification, 11% yield) using a combination of classical techniques and medium pressure ion-exchange chromatography. It is a dimeric enzyme of monomer molecular weight 50 000 and has no specific requirement for divalent metal ions. It has a high specificity for β-glucosides and hydrolyses a wide variety of different chemical types with retention of configuration at the anomeric centre. It has no exo-β-1,4-glucanase activity. It is reversibly inhibited by a variety of sugars which have been shown previously to be very active against glucosidases, suggesting a normal mechanism of action. Measured Km values for cellobiose and p-nitrophenyl β-D-glucopyranoside are quite low (0.70 and 0.08 mM, respectively), making this a good choice for cocloning into a cellulase system optimized for glucose production.


2014 ◽  
Vol 50 (6) ◽  
pp. 580-587 ◽  
Author(s):  
N. Arbsuwan ◽  
P. Sirithorn ◽  
S. Daduang ◽  
A. Dhiravisit ◽  
S. Thammasirirak

1993 ◽  
Vol 28 (2-3) ◽  
pp. 277-289 ◽  
Author(s):  
Viara N. Ivanova ◽  
Elena P. Dobreva ◽  
Elka I. Emanuilova

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