0.857
IF5
0.900
IF
Q3
JCR
0.92
CiteScore
0.405
SJR
Q2
SJR
20
MNiSW
165.24
ICV
ORIGINAL PAPER
 
CC-BY 4.0
 
 

Characterization of the amylolytic properties of the rumen ciliate protozoan Eudiplodinium maggii

G. Bełżecki 1  ,  
C. J. Newbold 2,  
N. R. McEwan 2,  
 
1
The Kielanowski Institute of Animal Physiology and Nutrition, Polish Academy of Sciences, 05-110 Jabłonna, Poland
2
Institute of Rural Sciences University, Aberystwyth, Llanbadarn Campus, Aberystwyth, SY23 3AL, Wales
3
Rowett Research Institute, Greenburn Road, Bucksburn, Aberdeen AB21 9SB, Scotland
J. Anim. Feed Sci. 2007;16(4):590–606
Publish date: 2007-11-21
KEYWORDS
ABSTRACT
The rumen ciliates Eudiplodinium maggii are thought to be strongly celluloloytic. We observed, however, that they preferentially ingested starch when the sheep were fed hay and ground barley. The studies reported in this paper were undertaken in order to characterize the amylolytic activity of these protozoa. The crude enzyme preparation obtained from the bacteria-free ciliates degraded starch and dextrin at the rate of 29.5 and 19.4 μmol released glucose/mg protein/h, respectively, while the degradation rate of maltose and isomaltose was only 0.45 and 0.14 μmol released glucose/mg protein/h. The pH and temperature optimum of starch, dextrin, maltose and isomaltose hydrolysis varied in the range of 4.5-7.5 and 45-55ºC relative to substrate. Pullulan was not degraded. Four protein bands with the ability to degrade starch were identified by a zymogram technique following the electrophoretic separation of protozoal protein. The enzymes were α-amylase in nature, as they degraded starch mainly to maltose and maltotriose. Ion-exchange chromatography of a crude enzyme preparation resulted in the separation of numerous fractions which were able to degrade starch. The most amylolytic fractions were very rich in protein and also exhibited a strong ability to digest carboxymethylcellulose. Partial sequences from two genes coding for synthesis of α-mylase enzymes were identified in a cDNA library of Eudiplodinium maggii. The rest of the sequences were reconstructed using GeneRacer and both complete genes were sequenced and cloned. Gene amyl 1 consisted of 1625 bp and the amyla 2 - 1593 bp. They encoded enzymes of 505 and 431 amino acids, respectively.
CORRESPONDING AUTHOR
G. Bełżecki   
The Kielanowski Institute of Animal Physiology and Nutrition, Polish Academy of Sciences, 05-110 Jabłonna, Poland
 
CITATIONS (9):
1. The ability of the rumen ciliate protozoan Diploplastron affine to digest and ferment starch
K. Wereszka, T. Michałowski
Folia Microbiologica
2. The Role of Ciliate Protozoa in the Rumen
Charles J. Newbold, Gabriel de la Fuente, Alejandro Belanche, Eva Ramos-Morales, Neil R. McEwan
Frontiers in Microbiology
3. The ability of rumen ciliates, Eudiplodinium maggii, Diploplastron affine, and Entodinium caudatum, to use the murein saccharides
G. Belzecki, R. Miltko, E. Kwiatkowska, T. Michalowski
Folia Microbiologica
4. Effect of Entodinium caudatum on starch intake and glycogen formation by Eudiplodinium maggii in the rumen and reticulum
Grzegorz Bełżecki, Neil R. McEwan, Barbara Kowalik, Tadeusz Michałowski, Renata Miltko
European Journal of Protistology
5. The ability of the rumen protozoan Eudiplodinium maggii to utilize chitin
R. Miltko, G. Bełżecki, E. Kwiatkowska, T. Michałowski
Folia Microbiologica
6. Can fungal zoospores be the source of energy for the rumen protozoa Eudiplodinium maggii?
Renata Miltko, Grzegorz Bełżecki, Barbara Kowalik, Tadeusz Michałowski
Anaerobe
7. Isolation and in vitro cultivation of the fibrolytic rumen ciliate Eremoplastron (Eudiplodinium) dilobum
Renata Miltko, Marta Pietrzak, Grzegorz Bełżecki, Krzysztof Wereszka, Tadeusz Michałowski, Johannes H.P. Hackstein
European Journal of Protistology
8. Mureinolytic ability of the rumen ciliate Diploplastron affine
G. Bełżecki, R. Miltko, E. Kwiatkowska, T. Michałowski
Folia Microbiologica
9. The ciliate, Troglodytella abrassarti, contributes to polysaccharide hydrolytic activities in the chimpanzee colon
I. Profousová, K. Mihaliková, T. Laho, Z. Váradyová, K. J. Petrželková, D. Modrý, S. Kišidayová
Folia Microbiologica
ISSN:1230-1388