Abstract
Growth patterns on and utilization of various alpha-glucans were investigated in Pseudomonas amyloderamosa and P. saccharophila. Maltose, maltodextrins (average chain length 7 glycosyl units) and glycogen supported excellent growth of both organisms and were extensively metabolized, although glycogen utilization in P. saccharophila was preceded by a prolonged lag phase. P. amyloderamosa produced limited growth on amylopectin and the carbohydrate was only partly degraded. It seemed likely that many of the unit chains liberated from amylopectin had a length exceeding the substrate range accepted by the maltodextrin permease (transport) system. A correlation was established between the pH of the medium and the utilization of glycogen and amylopectin for growth in P. amyloderamosa. The carbohydrates were at least partly utilizable at pH 6.0, whereas they could not support any growth at pH 6.5. Most likely, the lack of growth at the higher pH reflected the low activity of isolamylase at this pH. The enzyme patterns of maltodextrin catabolism in the two bacteria were established. Intracellularly, maltodextrin phosphorylase and 4-alpha-glucanotransferase occurred in both. Degradation of extracellular alpha-glucans was mediated by a mainly intracellular isoamylase in P. amyloderamosa, whereas P. saccharophila possessed an extracellular alpha-amylase and a firmly cell-bound pullulanase.
MeSH Terms
Amylases/metabolism
Amylopectin/metabolism
Detergents
Dextrins/metabolism
Glucose/metabolism
Glucosyltransferases/metabolism
Glycogen/metabolism
Hydrogen-Ion Concentration
Isoamylase/metabolism
Maltose/metabolism
Phosphorylases/metabolism
Polysaccharides/metabolism
Pseudomonas/enzymology,metabolism
Species Specificity
Chemicals
Detergents
Dextrins
Polysaccharides
Maltose
Glycogen
Amylopectin
Glucosyltransferases
Phosphorylases
Amylases
Isoamylase
Glucose
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Norrman J
Wöber G
References (13)
13 references, click to expand
-
Purification and properties of Pseudomonas isoamylase.
Biochim Biophys Acta. 1970 Sep 16;212(3):458-69
PMID: 5456995
-
A glycogen-debranching enzyme from Cytophaga.
FEBS Lett. 1970 Dec 28;12(2):96-100
PMID: 11945550
-
Pullulan, a relationship between molecular weight and fine structure.
FEBS Lett. 1970 Oct 5;10(3):190-193
PMID: 11945391
-
Detection of sugars on paper chromatograms.
Nature. 1950 Sep 9;166(4219):444-5
PMID: 14775715
-
Purification, crystallization, and properties of the alpha-amylase of Pseudomonas saccharophila.
Biochim Biophys Acta. 1956 Feb;19(2):267-73
PMID: 13315270
-
The action pattern of amylomaltase.
FEBS Lett. 1968 Jul;1(1):1-3
PMID: 11945237
-
The amylases of pseudomonas saccharophila.
J Bacteriol. 1953 Dec;66(6):656-63
PMID: 13117790
-
Protein measurement with the Folin phenol reagent.
J Biol Chem. 1951 Nov;193(1):265-75
PMID: 14907713
-
Formation of isoamylase by Pseudomonas.
Appl Microbiol. 1968 Oct;16(10):1439-44
PMID: 5684197
-
The pathway of exogenous and endogenous carbohydrate utilization in Escherichia coli: a dual function for the enzymes of the maltose operon.
Eur J Biochem. 1973 Nov 15;39(2):601-12
PMID: 4590453
-
[Pullulanase from Aerobacter aerogenes. Localization of the enzyme bound to continuously grown cells. Possible association with the outer membrane system of the cells].
Arch Mikrobiol. 1970;71(4):331-52
PMID: 5428605
-
Escherichia coli polyglucose phosphorylases.
Arch Biochem Biophys. 1968 Sep 20;127(1):164-74
PMID: 4878694
-
The pathway of maltodextrin metabolism in Pseudomonas stutzeri.
Hoppe Seylers Z Physiol Chem. 1973 Jan;354(1):75-82
PMID: 4807790