Biologia - 2008, Vol. 63, Iss. 6 - It has already appeared at SpringerLink:

http://www.springerlink.com/content/0006-3088

 

 

 

Editorial - Proceedings of the 3rd Symposium on the Alpha-Amylase Family, Smolenice Castle, Slovakia, September 23–27, 2007

 

Janecek S.

 

Biologia 2008, 63: 963-966. [PDF] DOI: 10.2478/s11756-008-0180-2

 

 

 

An enzyme family reunion – similarities, differences and eccentricities in actions on alpha-glucans.

 

Seo E.S., Christiansen C., Abou Hachem M., Nielsen M.M., Fukuda K., Bozonnet S., Blennow A., Aghajari N., Haser R. & Svensson B.

 

Biologia 2008, 63:: 967-979. [PDF] DOI: 10.2478/s11756-008-0164-2

 

 

 

Mechanisms involved in the biosynthesis of polysaccharides.

 

Robyt J.F.

 

Biologia 2008, 63: 980-988. [PDF] DOI: 10.2478/s11756-008-0168-y

 

 

 

Amylase action pattern on starch polymers.

 

Bijttebier A., Goesaert H. & Delcour J.A.

 

Biologia 2008, 63: 989-999. [PDF] DOI: 10.2478/s11756-008-0169-x

 

 

 

Structure-function relationship of substrate length specificity of dextran glucosidase from Streptococcus mutans.

 

Saburi W., Hondoh H., Kim Y.M., Mori H., Okuyama M. & Kimura A.

 

Biologia 2008, 63: 1000-1005. [PDF] DOI: 10.2478/s11756-008-0165-1

 

 

 

Differences and similarities in enzymes from the neopullulanase subfamily isolated from thermophilic species.

 

Nordberg Karlsson E., Labes A., Turner P., Fridjonsson O.F., Wennerberg C., Pozzo T., Hreggvidson G.O., Kristjansson J.K. & Schoenheit P.

 

Biologia 2008, 63: 1006-1014. [PDF] DOI: 10.2478/s11756-008-0171-3

 

 

 

Sucrose phosphorylases catalyze transglycosylation reactions on carboxylic acid compounds.

 

Sugimoto K., Nomura K., Nishiura H., Ohdan K., Nishimura T., Hayashi H. & Kuriki T.

 

Biologia 2008, 63: 1015-1019. [PDF] DOI: 10.2478/s11756-008-0161-5

 

 

 

Bacterial sucrose isomerases: properties and structural studies.

 

Rhimi M., Haser R. & Aghajari N.

 

Biologia 2008, 63: 1020-1027. [PDF] DOI: 10.2478/s11756-008-0166-0

 

 

 

Structure-function relationships in human salivary alpha-amylase: role of aromatic residues in a secondary binding site.

 

Ragunath C., Manuel S.G.A., Kasinathan C. & Ramasubbu N.

 

Biologia 2008, 63: 1028-1034. [PDF] DOI: 10.2478/s11756-008-0163-3

 

 

 

Role of the phenylalanine 260 residue in defining product profile and alcoholytic activity of the alpha-amylase AmyA from Thermotoga maritima.

 

Damian-Almazo J.Y., Lopez-Munguia A., Soberon-Mainero X. & Saab-Rincon G.

 

Biologia 2008, 63: 1035-1043. [PDF] DOI: 10.2478/s11756-008-0170-4

 

 

 

Proteolysis of alpha-amylase from Saccharomycopsis fibuligera: characterization of digestion products.

 

Hasan K., Tirta Ismaya W., Kardi I., Andiyana Z., Kusumawidjaya S., Ishmayana S., Subroto T. & Soemitro S.

 

Biologia 2008, 63: 1044-1050. [PDF] DOI: 10.2478/s11756-008-0167-z

 

 

 

An investigation on acarbose inhibition and the number of active sites in an amylopullulanase (L14–APU) from an Iranian Bacillus sp.

 

Ghollasi M., Khajeh K., Mollania N., Zareian S. & Naderi-Manesh H.

 

Biologia 2008, 63: 1051-1056. [PDF] DOI: 10.2478/s11756-008-0174-0

 

 

 

Domain evolution in the GH13 pullulanase subfamily with focus on the carbohydrate-bindingmodule family 48.

 

Machovic M. & Janecek S.

 

Biologia 2008, 63: 1057-1068. [PDF] DOI: 10.2478/s11756-008-0162-4