Candida Molischiana Research Articles

Detoxification of cassava pulp using Brevibacterium sp. R312

Brevibacterium sp. strain R312 has an endocellular β-glucosidase, a nitrile hydratase and an amidase that can break down some cyanoglucosides. Nonsterile cassava pulp suspensions were fermented using this strain and 70%–80% reduction of nitrile compounds, in particular cyanoglucosides and α-hydroxynitriles, was observed. This type of nitrile-hydratase-active microorganism could be a solution for the detoxification of cassava. Experiments conducted with the yeast Candida molischiana and C. wickkerhamii showed no improvement in detoxification.

Hydrolysis of grape monoterpenyl glycosides by Candida molischiana and Candida wickerhamii β‐glucosidases

AbstractThe exocellular β‐glucosidases of Candida molischiana and Candida wickerhamii are able to hydrolyse geranyl, neryl, citronellyl, linalyl and α‐terpinyl‐β‐D‐glucopyranosides. The nature of the aglycone residue greatly affects the rate of hydrolysis. Glucosides with a tertiary alcohol as aglycone residue are more slowly hydrolysed than those with a primary alcohol. The β‐glucosidase from C molischiana is also able to hydrolse α‐L‐arabinofuranosides. This results in the release of monoterpenols from a glycoside extract from grape juice.

Candida populi, a New Species of Yeast Occurring in Exudates of Populus and Betula Species

During a survey of yeasts occurring in exudates of various tree species in the Pacific Northwest of North America, 24 strains of an imperfect yeast were isolated in a wide geographic area, mainly from species of the genus Populus. The isolates were studied by traditional as well as molecular methods, and the results revealed a new species of the genus Candida. The new species is named Candida populi, because its principal habitat is in exudates of Populus species. C. populi resembles Candida molischiana but differs from this species in habitat, guanine-plus-cytosine content of the nuclear deoxyribonucleic acid, maximum growth temperature, and ability to assimilate several carbon compounds. The type strain of C. populi is strain UCD-FST 68-675B (= CBS 7351 = ATCC 64933).

Purification and properties of an exocellular β-glucosidase of Candida molischiana (Zikes) Meyer and Yarrow capable of hydrolyzing soluble cellodextrins

The exocellular enzyme β-glucosidase of Candida molischiana was studied. This strain is able to ferment soluble cellodextrins. The enzyme was partially purified by ion-exchange chromatography and gel filtration. The molecular weight of this enzyme was 120 000; its optimum pH was between 4 and 4.5 and its optimum temperature was 60 °C. This enzyme was active against different soluble glucosides and was inhibited by p-chloromercuribenzoate, gluconolactone, and glucose. A "glucosyltransferase" activity appeared in the presence of ethanol. The biosynthesis of the enzyme was constitutive but repressed by glucose.

Further taxonomic study of methanol-assimilating yeasts with special references to electrophoretic comparison of enzymes.

An electrophoretic comparison was made of 13 enzymes in 53 strains of methanol-assimilating yeasts. Nine strains of Candida boidinii were divided into two closely related interspecific clusters. The methanol-assimilating Hansenula yeasts showed electrophoretic patterns of enzymes very similar to one another, suggesting a close interrelationship. Pichia lindnerii and Candida methanolovescens showed similar physiological and chemotaxonomic characteristics, but they differed in the electrophoretic patterns of their enzymes. Pichia methanolica and three strains of Pichia cellobiosa showed the same electrophoretic patterns and chemotaxonomic characteristics. Eleven strains of Hansenula capsulata and its supposed anamorph Candida molischiana showed different electrophoretic patterns of enzymes and DNA base composition. They were divided into 5 clusters on the basis of these characteristics. The facts suggest the heterogeneity of these species. It would not be appropriate to regard C. molischiana simply as an anamorph of H. capsulata. The electrophoretic patterns of the enzymes exhibited a good correlation with the groups of methanol-assimilating yeasts, based on the DNA base composition, the coenzyme Q systems, and the proton magnetic resonance spectra of cell-wall mannans.