Catalytic properties and mode of action of endo-(1-->3)-beta-D-glucanase and beta-D-glucosidase from the marine mollusk Littorina kurila.

3)-beta-D-glucanase and beta-D-glucosidase from the marine mollusk Littorina kurila. -->
Autoři: Pesentseva MS; Pacific Institute of Bioorganic Chemistry, Far East Branch of Russian Academy of Sciences, 690022 Vladivostok, 159 Prospect 100 let Vladivostoku, Russia., Kusaykin MI, Anastyuk SD, Sova VV, Zvyagintseva TN
Zdroj: Carbohydrate research [Carbohydr Res] 2008 Sep 22; Vol. 343 (14), pp. 2393-400. Date of Electronic Publication: 2008 Jul 06.
Způsob vydávání: Journal Article; Research Support, Non-U.S. Gov't
Jazyk: English
Informace o časopise: Publisher: Elsevier Country of Publication: Netherlands NLM ID: 0043535 Publication Model: Print-Electronic Cited Medium: Print ISSN: 0008-6215 (Print) Linking ISSN: 00086215 NLM ISO Abbreviation: Carbohydr Res Subsets: MEDLINE
Imprint Name(s): Publication: Amsterdam : Elsevier
Original Publication: Amsterdam.
Výrazy ze slovníku MeSH: Endo-1,3(4)-beta-Glucanase/*metabolism , Glucosidases/*metabolism , Snails/*enzymology, Animals ; Endo-1,3(4)-beta-Glucanase/chemistry ; Endo-1,3(4)-beta-Glucanase/isolation & purification ; Glucans ; Glucosidases/chemistry ; Glucosidases/isolation & purification ; Hydrogen-Ion Concentration ; Hydrolysis ; Liver/enzymology ; Marine Biology ; Molecular Weight ; Nuclear Magnetic Resonance, Biomolecular ; Polysaccharides/metabolism ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Substrate Specificity
Abstrakt: A complex of the enzymes from the liver of the marine mollusk Littorina kurila that hydrolyzes laminaran was investigated. Two (1-->3)-beta-d-glucanases (G-I and G-II) were isolated. The molecular mass of G-I as estimated by gel-permeation chromatography and SDS-PAGE analysis was 32 and 40kDa, respectively. The G-II molecular mass according to SDS-PAGE analysis was about 200kDa. The pH optimum for both G-I and G-II was pH 5.4. The G-I had narrow substrate specificity and hydrolyzed only the (1-->3)-beta-d-glucosidic bonds in the mixed (1-->3),(1-->6)- and (1-->3),(1-->4)-beta-d-glucans down to glucose and glucooligosaccharides. This enzyme acted with retention of the anomeric configuration and catalyzed a transglycosylation reaction. G-I was classified as the glucan endo-(1-->3)-beta-d-glucosidase (EC 3.2.1.39). G-II exhibited both exo-glucanase and beta-d-glucoside activities. This enzyme released from the laminaran glucose as a single product, but retained the anomeric center configuration and possessed transglycosylation activity. The hydrolysis rate of glucooligosaccharides by G-I decreased with an increase of the substrate's degree of polymerization. In addition to (1-->3)-beta-d-glucanase activity, the enzyme had the ability to hydrolyze p-nitrophenyl beta-d-glucoside and beta-d-glucobioses: laminaribiose, gentiobiose, and cellobiose, with the rate ratio of 50:12:1. G-II may correspond to beta-d-glucoside glucohydrolase (EC 3.2.1.21).
Substance Nomenclature: 0 (Glucans)
0 (Polysaccharides)
9008-22-4 (laminaran)
EC 3.2.1.- (Glucosidases)
EC 3.2.1.6 (Endo-1,3(4)-beta-Glucanase)
Entry Date(s): Date Created: 20080805 Date Completed: 20081203 Latest Revision: 20151119
Update Code: 20231215
DOI: 10.1016/j.carres.2008.06.025
PMID: 18675406
Autor: Pesentseva MS; Pacific Institute of Bioorganic Chemistry, Far East Branch of Russian Academy of Sciences, 690022 Vladivostok, 159 Prospect 100 let Vladivostoku, Russia., Kusaykin MI, Anastyuk SD, Sova VV, Zvyagintseva TN
Jazyk: angličtina
Zdroj: Carbohydrate research [Carbohydr Res] 2008 Sep 22; Vol. 343 (14), pp. 2393-400. Date of Electronic Publication: 2008 Jul 06.
DOI: 10.1016/j.carres.2008.06.025
Abstrakt: A complex of the enzymes from the liver of the marine mollusk Littorina kurila that hydrolyzes laminaran was investigated. Two (1-->3)-beta-d-glucanases (G-I and G-II) were isolated. The molecular mass of G-I as estimated by gel-permeation chromatography and SDS-PAGE analysis was 32 and 40kDa, respectively. The G-II molecular mass according to SDS-PAGE analysis was about 200kDa. The pH optimum for both G-I and G-II was pH 5.4. The G-I had narrow substrate specificity and hydrolyzed only the (1-->3)-beta-d-glucosidic bonds in the mixed (1-->3),(1-->6)- and (1-->3),(1-->4)-beta-d-glucans down to glucose and glucooligosaccharides. This enzyme acted with retention of the anomeric configuration and catalyzed a transglycosylation reaction. G-I was classified as the glucan endo-(1-->3)-beta-d-glucosidase (EC 3.2.1.39). G-II exhibited both exo-glucanase and beta-d-glucoside activities. This enzyme released from the laminaran glucose as a single product, but retained the anomeric center configuration and possessed transglycosylation activity. The hydrolysis rate of glucooligosaccharides by G-I decreased with an increase of the substrate's degree of polymerization. In addition to (1-->3)-beta-d-glucanase activity, the enzyme had the ability to hydrolyze p-nitrophenyl beta-d-glucoside and beta-d-glucobioses: laminaribiose, gentiobiose, and cellobiose, with the rate ratio of 50:12:1. G-II may correspond to beta-d-glucoside glucohydrolase (EC 3.2.1.21).
Databáze: MEDLINE
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