Yeast Spheroplasts Formed by Cell Wall-Degrading Enzymes from
            <i>Oerskovia</i>
            sp

Mann, J. W.; Heintz, C. E.; Macmillan, James D.

doi:10.1128/jb.111.3.821-824.1972

Cited by 22 publications

(9 citation statements)

References 12 publications

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“…The strongly lytic culture fluid of an Oerskovia sp. (25) probably contains this type of glucanase. It has now been established that B. circulans WL-12 also produces a lytic-type ,-(1 -_ 3)-glucanase (F. M. Rombouts and H. J. Phaff, unpublished results), which is currently under investigation.…”

Section: Discussionmentioning

confidence: 97%

“…Not understood at present is how the lytic j3-(1 --3)-glucanases have access to the wall glucans. The action of these enzymes is not prevented by the outer mannan layer of the wall since they are capable of eliciting protoplast formation from intact yeast cells (23,25,50). Further information is required about the action and properties of the lytic ,B-(1 _ 3)-glucanase.…”

Section: Discussionmentioning

confidence: 99%

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Lysis of Yeast Cell Walls: Glucanases from Bacillus circulans WL-12

Fleet

Phaff

1974

J Bacteriol

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Endo--(1 -3)-and endo-#-(1 -6)-glucanases are produced in high concentration in the culture fluid of Bacillus circulans WL-12 when grown in a mineral medium with bakers' yeast cell walls as the sole carbon source. Much lower enzyme levels were found when laminarin, pustulan, or mannitol was the substrate. The two enzyme activities were well separated during Sephadex G-100 chromatography. The endo-,-(1 -3)-glucanase was further purified by diethylaminoethyl-cellulose and hydroxyapatite chromatography, whereas the endo-#-(1 -d 6)-glucanase could be purified further by diethylamino-ethyl-cellulose and carboxymethyl cellulose chromatography. The endo-ft-(1 -. 3)-glucanase was specific for the ,-(1 -_ 3)-glucosidic bond, but it did not hydrolyze laminaribiose; laminaritriose was split very slowly. #-(1 -4)-Bonds in oat glucan in which the

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Section: Discussionmentioning

confidence: 97%

Section: Discussionmentioning

confidence: 99%

Lysis of Yeast Cell Walls: Glucanases from Bacillus circulans WL-12

Fleet

Phaff

1974

J Bacteriol

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“…Since a commercial preparation of chitinase also contained potent /8(1-)3)-glucanase activity (31), it was considered advisable to prepare and characterize a(1-*+3)-glucanase, f(1-3)glucanase, and chitinase. Although other microbial sources of a(1-3)-glucanases (9,11,13) and f8(1-)3)-glucanase (25,35) were known, the presence of an inducer was required to obtain appreciable yields, whereas C. resinae was a constitutive producer of these two activities when the carbon source for growth was mannitol. a-and 18-glucanases were separated (34), and the problem of concurrent chitinase secretion was minimized by mass adsorption.…”

Section: Discussionmentioning

confidence: 99%

“…The protease, Pronase CB (Calbiochem), was incubated with cell wall samples for varying times at 370C in a 0.05 M tris(hydroxymethyl)aminomethanehydrochloride buffer, pH 7.5, containing, per milliliter: CaCl2, 555 ,ug; cycloheximide, 50 ug; and chloramphenicol, 25 .g. The amino acid so liberated was estimated with ninhydrin.…”

Section: Methodsmentioning

confidence: 99%

Serial enzymatic hydrolysis of cell walls of two serotypes of yeast-form Histoplasma capsulatum with alpha(1 leads to 3)-glucanase, beta(1 leads to 3)-glucanase, pronase, and chitinase

Reiss¹

1977

Infect Immun

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A serial enzymatic hydrolysis procedure for the partial lysis of Histoplasma capsulatum yeast-form cell walls was described, and its application for the differentiation of two serotypes was evaluated. Cell walls were serially digested with alpha(1 leads to 3)-glucanase and beta(1 leads to 3)-glucanse of Cladosporium resinae, then by Pronase, and then by chitinase. The walls of serotype 1, 2, 3 (61.5% digested) were not susceptible to alpha(1 leads to 3)-glucanse, and they contained 30.3% chitin, thus identifying the strain as chemotype 1 (chem 1). Serotype 1, 4 cells walls (51.6% digested) released 27.3% as glucose after treatment with alpha(1 leads to 3)-glucanse and contained 7.8% chitin, compatible with chemotype 2 (chem 2). In addition to quantitating the monomeric products of enzymolysis, I recovered soluble nondialyzable polysaccharide from the digests of both serotypes.

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“…In a preliminary note (10) we reported that an Oerskovia species isolated from soil produces inducible extracellular enzymes that rapidly degrade the walls of various yeasts. Enzyme action on viable cells lyses them or forms spheroplasts depending on osmotic conditions.…”

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confidence: 99%

Production and Ecological Significance of Yeast Cell Wall-Degrading Enzymes from Oerskovia

Mann

Jeffries

Macmillan

1978

Appl Environ Microbiol

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Motile actinomycetes capable of degrading walls of viable yeast cells were isolated from soil and identified as Oerskovia xanthineolytica. A lytic assay based on susceptibility of enzyme-treated cells to osmotic shock was developed, and 10 of 15 strains of 0. xanthineolytica, Oerskovia turbata, and nonmotile Oerskovialike organisms from other collections were found to possess yeast lytic activities. All lytic strains produced laminaranase and a-mannanase, but the amounts, determined by reducing group assays, were not proportional to the observed lytic activities. The Oerskovia isolates demonstrated chemotactic, predatory activity against various yeast strains and killed yeasts in mixed cultures. Of 15 carbon sources tested for production of lytic enzyme, purified yeast cell walls elicited the highest activity. Glucose repressed enzyme production and caused cells to remain in the microfilamentous and motile rod stages of the Oerskovia cell cycle. Crude lytic activity was optimal at pH 5.6 to 7.0 and inactivated by heating for 6 min at 50°C. Partial purification by isoelectric focusing showed that all lytic activity was associated with four f,-(1-3)-glucanases. The absence of protein disulfide reductase, N-acetyl-fB-D-hexosaminidase, and phosphomannanase in crude preparations indicated that the principal enzyme responsible for yeast wall lysis was a fi-(1-3)glucanase that produced relatively little reducing sugar from yeast glucan.

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Yeast Spheroplasts Formed by Cell Wall-Degrading Enzymes from Oerskovia sp

Abstract: Oerskovia sp. produces inducible extracellular enzymes which degrade the walls of various yeasts. Yeast spheroplasts are formed from both log- and stationary-phase cells.

Cited by 22 publications

References 12 publications

Lysis of Yeast Cell Walls: Glucanases from Bacillus circulans WL-12

Lysis of Yeast Cell Walls: Glucanases from Bacillus circulans WL-12

Serial enzymatic hydrolysis of cell walls of two serotypes of yeast-form Histoplasma capsulatum with alpha(1 leads to 3)-glucanase, beta(1 leads to 3)-glucanase, pronase, and chitinase

Production and Ecological Significance of Yeast Cell Wall-Degrading Enzymes from Oerskovia

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