Utilization of lactose in non-respiring cells of the yeast Debaryomyces polymorphus

1986 ◽  
Vol 145 (4) ◽  
pp. 367-371 ◽  
Author(s):  
Barbara Schulz ◽  
Milan H�fer
Keyword(s):  
Debaryomyces Polymorphus

Debaryomyces polymorphus and D. pseudo-polymorphus, New Taxonomic Combinations

Mycologia ◽  
1979 ◽  
Vol 71 (2) ◽  
pp. 444 ◽  
Author(s):  
C. W. Price ◽  
H. J. Phaff
Keyword(s):  
Debaryomyces Polymorphus

scholarly journals Decolorization of an azo dye, Reactive Black 5 and MnP production by yeast isolate: Debaryomyces polymorphus

2005 ◽  
Vol 24 (3) ◽  
pp. 249-253 ◽  
Author(s):  
Qingxiang Yang ◽  
Ayfer Yediler ◽  
Min Yang ◽  
Antonius Kettrup
Keyword(s):  
Azo Dye ◽  
Reactive Black 5 ◽  
Yeast Isolate ◽  
Debaryomyces Polymorphus

scholarly journals Debaryomyces polymorphus var. africanus, a new variety of ascosporogenous yeast found in South Africa.

1994 ◽  
Vol 40 (4) ◽  
pp. 331-337 ◽  
Author(s):  
JOHANNES P. VAN DER WALT ◽  
TAKASHI NAKASE ◽  
MOTOFUMI SUZUKI ◽  
MASAKO TAKASHIMA ◽  
YUZO YAMADA
Keyword(s):  
South Africa ◽  
New Variety ◽  
Ascosporogenous Yeast ◽  
Debaryomyces Polymorphus

L-Rhamnose metabolism in Pichia stipitis and Debaryomyces polymorphus

1994 ◽  
Vol 40 (11) ◽  
pp. 896-902 ◽  
Author(s):  
A. L. Twerdochlib ◽  
F. O. Pedrosa ◽  
S. Funayama ◽  
L. U. Rigo
Keyword(s):  
Carbon Source ◽  
Aldehyde Dehydrogenase ◽  
Enzyme Induction ◽  
Catabolite Repression ◽  
Sole Carbon Source ◽  
Pichia Stipitis ◽  
Oxidative Pathway ◽  
Debaryomyces Polymorphus

The pathway for the breakdown of L-rhamnose by the yeast Pichia stipitis NRC 5568 was shown to involve nonphosphorylated intermediates and to produce pyruvate and L-lactaldehyde. The activities of the enzymes and the nature of several intermediates were determined. The enzymes involved are L-rhamnose dehydrogenase, L-rhamnonate dehydratase, and 2-keto-3-deoxy-L-rhamnonate aldolase. This pathway was found to be inducible by L-rhamnose and repressed by D-glucose. These enzymes were also present in a mutant of P. stipitis (PR1) resistant to catabolite repression and in Debaryomyces polymorphus 1747. Cell-free extracts of P. stipitis and D. polymorphus grown in L-rhamnose as sole carbon source were found to contain NAD+-dependent aldehyde dehydrogenase activities.Key words: Pichia stipitis, enzyme induction, oxidative pathway, catabolite repression.

Nuclear behaviour accompanying ascus formation in Debaryomyces polymorphus

1987 ◽  
Vol 33 (11) ◽  
pp. 967-970 ◽  
Author(s):  
Sharon I. Forrest ◽  
Carl F. Robinow ◽  
Marc-André Lachance
Keyword(s):  
Light Microscopy ◽  
Cross Wall ◽  
Parent Cell ◽  
The Cross ◽  
Nuclear Behaviour ◽  
Debaryomyces Polymorphus

Nuclear behaviour in growing, dividing, and ascospore-forming cells of a strain of Debaryomyces polymorphus, a member of the "Torulaspora group" of yeasts, has been studied by light microscopy of fixed Giemsa-stained preparations. Many of the images seen were compatible with the suggestion, advanced by certain earlier students, that meiosis in this type of yeast is preceded by a process of self-diploidization involving the nucleus of a bud that, despite its small size, is already separated from the parent cell by a cross wall. Diploidization, in this view, is achieved by the return of the bud nucleus to the parent cell via a channel in the cross wall. The bud nucleus next fuses with the nucleus of the parent cell. Self-diploidization in D. polymorphus is thus achieved in the guise of heterogamous conjugation. This in turn is followed by meiosis. A lesser number of cell associations suggestive of isogamous conjugation has been encountered also.

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