Lysis of viable yeast cells by enzymes of Arthrobacter luteus

Kitamura, Kumpei; Kaneko, Tatsuhiko; Yamämoto, Yasushi

doi:10.1016/0003-9861(71)90053-1

Cited by 109 publications

(40 citation statements)

References 17 publications

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“…Zymolyase contains both a protease with affinity for mannoproteins and b-1,3-glucanase, which releases pentasaccharides from pachyman or laminarin. [29] The actions of both enzymes are required to lyse yeast cells. The course of lysis can be followed as a function of the The cells cannot maintain homeostasis, and they burst without the cell walls.…”

Section: Methodsmentioning

confidence: 99%

Yeast Cells with an Artificial Mineral Shell: Protection and Modification of Living Cells by Biomimetic Mineralization

et al. 2008

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Section: Methodsmentioning

confidence: 99%

Yeast Cells with an Artificial Mineral Shell: Protection and Modification of Living Cells by Biomimetic Mineralization

et al. 2008

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“…A highly lytic representative of this group was isolated from the culture liquid of Cytoplzuga johnsonii [22]. Other examples are the lytic p-( 1 + 3)-glucanase "zymolyase" from Arthrobacter luteus [23,24] and from another Arthrohacter strain [18,. Also, fungal enzymes of this type have been reported [28 -301.…”

Section: Properties Of P-(l-+3)-glucunases and Their Action On Yeast mentioning

confidence: 99%

Lysis of Yeast Cell Walls

Rombouts¹,

Phaff

1976

European Journal of Biochemistry

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Bacillus circulans WL-12, when grown in a mineral medium with yeast cell walls or yeast glucan as the sole carbon source, produced five 8-glucanases. Two /?-(1-+3)-glucanases (I and 11), which are lytic to yeast cell walls, were isolated from the culture liquid by batch adsorption on yeast glucan, and separated by chromatography on hydroxylapatite. Lytic /?-( 1 + 3)-glucanase I was further purified by carboxymethylcellulose chromatography. The specific activity of lytic P-( 1 -+ 3)-glucanase I on laminarin was 4.1 U per mg of protein. The enzyme moved as a single protein with a molecular weight of 40000 during sodium dodecylsulfate electrophoresis in slab gels. It was specific for the p-(1+3)-glucosidic bond but the enzyme did not hydrolyze laminaribiose. Hydrolysis of laminarin went through a series of oligosaccharides, and laminaribiose and glucose accumulated till the end of the reaction. A small amount of gentiobiose was also produced from laminarin. Products from yeast cell walls and yeast glucan included laminaripentaose, laminaritriose, laminaribiose, glucose, and gentiobiose, but no laminaritetraose was detected. This glucanase has an optimum pH of 5.5. Laminarin hydrolysis followed Michaelis-Menten kinetics. A K, of 0.105 mg of laminarin per ml and a V of 5.6 micro-equivalents of glucose released/min per mg enzyme protein were calculated. The enzyme required no metal ions. The lytic p-(1 --f 3)-glucanase I is a powerfully lytic enzyme, completely solubilizing the glucan of yeast cell walls. Synergism with lytic /?-( 1 +6)-glucanase could be observed during yeast glucan hydrolysis.Lytic B-( 1 -+3)-glucanase I1 could be further purified by carboxymethyl-cellulose and diethylamino-ethyl-agarose chromatography. At this stage lytic P-( 1 --f 3)-glucanase I1 was still contaminated with some non-lytic P-(1-+3)-glucanase that could not be removed by any further chromatographic steps. The enzyme has an optimum pH of 6.5 to 7; its properties were not studied further.Bacillus circulans WL-12 was isolated as an organism capable of degrading yeast cell walls [l]. It was found that this bacterium produces a number of P-glucanases when grown on bakers' yeast cell walls or on alkali-insoluble bakers' yeast glucan [l -31.Fleet and Phaff [2] isolated both a /?-(1+3)-and a P-(1 +6)-glucanase in highly purified form from the culture liquid, and observed that the hydrolytic action of these enzymes on isolated yeast cell walls was negligible. Neither of the enzymes nor the combination of the two could lyse cell walls to an extent that clearing could be observed in a cell wall agar plate. Also, the enzymes were unable to hydrolyze the microfibrillar glucan network present in Succharomyces walls [4]. The enzymes were therefore considered to be non-lytic. Subsequently, Rombouts and Phaff [3] found that lytic enzymes, which were present in the culture liquid of Bacillus circulans WL-12, could be -~ Enzyme. Endo-l,3-/~'-glucanase (EC 3.2.1.6).isolated by adsorption onto alkali-insoluble yeast glucan. Fractionation of the lytic p...

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“…, Rhi:::opUS, '3) Corticium, 14) Coprinus,'ul Cytophaga, '6) Physarum '7 ) and Sclerotinia. '8 ) Previously, 19,20) we reported that Arthrobacter luteus KI 1508 (B-lll-l) produced enzymes which lysed living yeast cells. The optimum pH for lysis of living yeast cells was 7.0-8.0.…”

Section: Notementioning

confidence: 99%