Production of Flower-Inducing Substance(s) by the Treatment of Lemna Extract with Some Commercial Enzyme Preparations

2002 ◽  
Vol 2002 ◽  
pp. 210-210 ◽  
Author(s):  
D. Colombatto ◽  
D.P. Morgavi ◽  
A.F. Furtado ◽  
K.A. Beauchemin

Results in the literature concerning the efficacy of feed enzymes for ruminant diets have been mixed. Commercial preparations currently used are fermentation extracts containing several enzymic activities. It has been suggested that ruminal fermentation of grass and maize silages is enzyme-limited (Wallace et al., 2001). In order to design better enzyme additives, the enzyme activities likely to affect the animal responses should be identified. This study examined 23 commercial enzyme preparations for their biochemical properties and their ability to influence the in vitro degradation of alfalfa and maize silage.


2000 ◽  
Vol 2000 ◽  
pp. 27-27 ◽  
Author(s):  
D. Colombatto ◽  
F. L. Mould ◽  
M. K. Bhat ◽  
E. Owen

Several techniques involving enzymes as alternatives to rumen fluid inin vitrostudies have been proposed. However, high cost, ill-defined characterisation and high variation among enzyme preparations and batches have discouraged their use. In addition, most studies have aimed at determining dry matter degradability (DMD) at a fixed time, commonly 48 h. Consequently little information has been published concerning the DM degradation dynamics of forages incubated with enzymes. Therefore the objective of the present study was to compare the ability of a commercial enzyme mixture to describe the fermentation dynamics of two contrasting forages, using the ANKOMin vitrofermentation system (Daisy II, ANKOM Co, USA).


2012 ◽  
pp. 169-180
Author(s):  
William S. Adney ◽  
Nancy Dowe ◽  
Edward W. Jennings ◽  
Ali Mohagheghi ◽  
John Yarbrough ◽  
...  

1980 ◽  
Vol 191 (1) ◽  
pp. 203-207 ◽  
Author(s):  
Y Oike ◽  
K Kimata ◽  
T Shinomura ◽  
S Suzuki

Significant amounts of proteinase activity have been found in chondroitin ABC lyase (EC 4.2.2.4), chondroitin AC II lyase and endo-beta-D-galactosidase (keratanase) from commercial sources. It would appear, therefore, that certain earlier biochemical and histochemical studies, which employed these commercial enzyme preparations for their presumed ability to degrade only glycosaminoglycans, may require re-evaluation. A mixture of EDTA, N-ethylmaleimide, phenylmethanesulphonyl fluoride and pepstatin abolishes the effect of the contaminating proteinases on proteoglycan with less significant effect on the chondroitin lyase or keratanase activity.


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