Purification of exo-1,3-beta-glucanase, a new extracellular glucanolytic enzyme from Talaromyces emersonii

2010 ◽  
Vol 89 (3) ◽  
pp. 685-696 ◽  
Author(s):  
Elaine O’Connell ◽  
Charles Piggott ◽  
Maria Tuohy
1992 ◽  
Vol 72 (1) ◽  
pp. 117-125 ◽  
Author(s):  
P. A. Thacker ◽  
G. L. Campbell ◽  
J. W. D. GrootWassink

Two experiments of a factorial design (sex × treatment) were conducted to determine the effects of enzyme and salinomycin supplementation on the nutritive value of barley or rye-based diets for growing pigs fed from approximately 20 to 85 kg. For exp. 1, 72 crossbred pigs were fed either a barley-based control diet or a similar diet supplemented with enzyme (Aspergillus niger; 750 units g−1 beta-glucanase and 650 units g−1 pentosanase), salinomycin (25 ppm) or both additives in combination. For exp. 2, two replicates of 48 pigs were fed either a barley-based diet, an unsupplemented rye-based diet or a rye-based diet supplemented with enzyme, salinomycin or both additives. During both experiments, chromic oxide (0.5%) was added to the diet of four to six pigs/treatment to act as a digestibility indicator starting when the pigs reached 42 kg. Neither enzyme nor salinomycin, alone or in combination, significantly improved the growth rate or feed efficiency of pigs fed barley or rye. Supplementation of barley with the combination of additives significantly (P < 0.05) improved protein digestibility while neither enzyme nor salinomycin had any effect on nutrient digestibility when fed alone. In rye-based diets, salinomycin, both alone and in combination, significantly (P < 0.05) improved the digestibility of crude protein and energy. Dry matter digestibility of the rye-based diets was unaffected by treatment. Key words: Swine, rye, barley, beta-glucanase, pentosanase, salinomycin


2020 ◽  
Author(s):  
Lekshmi K. Edison ◽  
N. S. Pradeep

AbstractScreening of potential soil actinomycetes is static at infant phase because less than one part of soil biodiversity has been explored. An important factor considered before isolating microorganisms with potential application is understanding the biodiversity and environmental features associated with growth. Search of distinctive enzymes from unusual ecological habitats are highly fascinating and have great opportunities that may also pointed the developments in high throughput screening programs. In the present study Western Ghats hot spot regions of Kerala has been explored for the actinomycetes strains with beta glucanase activity. A total of 127 actinomycetes strains were isolated. After qualitative primary screening 106 strains (83%) produced exo-β-1,4-glucanase enzyme and 79 strains (62%) produced endo-β-1,3-glucanase enzyme. The quantitative secondary screening confirmed the strains TBG-MR17 and TBG-AL13 recognised as respective dominant producers of exo-β-1,4-glucanase and endo-β-1,3-glucanase enzymes. The study reveals the richness of the Western Ghats soils with innumerable actinomycetes having potential β-glucanase activities.


1992 ◽  
Vol 283 (1) ◽  
pp. 31-34 ◽  
Author(s):  
M M Brooks ◽  
M G Tuohy ◽  
A V Savage ◽  
M Claeyssens ◽  
M P Coughlan

Three forms of exocellobiohydrolase (EC 3.2.1.91), CBH IA, CBH IB and CBH II, were isolated to apparent homogeneity from culture filtrates of the aerobic fungus Talaromyces emersonii. CBH IA and CBH II appear to be native forms of these enzymes, while CBH IB may represent a proteolytic degradation product of the CBH IA enzyme. The hydrolysis of beta-cellobiosyl fluoride by each form was monitored by 1H-n.m.r. spectroscopy. The reactions catalysed by CBH IA and CBH IB proceed with retention of the anomeric configuration, whereas that catalysed by CBH II is one of inversion. Thus one may deduce that CBH IA (or CBH IB) and CBH II operate double and single displacement reactions respectively during catalysis of substrate. On the basis of these findings and the observed substrate specificities of the various forms, one may conclude that CBH IA (and CBH IB) is a family C enzyme, while CBH II belongs to family B [Henrissat, Claeyssens, Tomme, Lemesle & Mornon (1989) Gene 81, 83-95].


1996 ◽  
Vol 93 (8) ◽  
pp. 3487-3491 ◽  
Author(s):  
L. G. Jensen ◽  
O. Olsen ◽  
O. Kops ◽  
N. Wolf ◽  
K. K. Thomsen ◽  
...  

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