Pectic Enzymes in Tissue Degradation

Bateman, and D F; Millar, R. L.

doi:10.1146/annurev.py.04.090166.001003

Cited by 301 publications

(108 citation statements)

References 40 publications

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“…The pectic enzymes which are formed by micro-organisms in plant tissue may differ from those formed in culture media (Bateman & Millar, 1966). For most of this work the cultures were grown in potato tissue in order to induce formation of enzymes important in the maceration of that tissue.…”

Section: Discussionmentioning

confidence: 99%

Pectic Enzymes of Pigmented Strains of Clostridium

Lund¹,

Brocklehurst²

1978

Journal of General Microbiology

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59The pectic enzymes of six strains of pigmented, pectolytic clostridia isolated from potatoes were examined and compared with those strains of Clostridium felsineum and Clostridium aurantibutyricum using cup-plate assays. The organisms could be divided into two groups. Group I consisted of the potato isolates and the strain of C. aurantibutyricum; these formed pectic lyase enzymes and pectinesterase but no pectic hydrolase. Group 2 consisted of eight strains of C. felsineum (and one culture labelled Clostridium roseum) ; these formed pectic lyase and pectic hydrolase but no detectable pectinesterase. Viscometric studies and analyses of degradation products of pectate formed by enzymes of four representative strains from group I and two strains from group 2 showed that all these clostridia formed endopectate lyase enzymes; studies of one enzyme preparation showed that the pH optimum was about 9-5. In addition, the group 2 organisms formed endopolygalacturonase and probably also exopolygalacturonase. I N T R O D U C T I O NDuring studies of bacterial soft rot of potatoes, pectolytic clostridia have regularly been detected in rotting tissue (Lund, 1972;Lund & Kelman, 1977). Although the primary cause of this spoilage is usually Erwinia carotovora, some of these pectolytic clostridia cause rapid maceration of potato tissue and undoubtedly enhance the effect of E. carotovora (Rudd-Jones & Dowson, 1950). The pectolytic clostridia associated with rotting potatoes probably belong to several species (Lund, 1972) and include a group of bacteria which form a pink pigment. Apart from the colour of the pigment, these clostridia have many properties in common with Clostridium felsineum (B. M. Lund & G. M. Wyatt, unpublished). The purpose of this work was to determine whether pigmented clostridia isolated from potatoes differed from C. felsineum or another pigmented clostridium, Clostridium aurantibutyricum, in the type of pectic enzymes formed.Of the bacterial enzymes which depolymerize pectic substances, the most widely reported are those with lyase activity, although bacteria from several genera form enzymes which hydrolyse pectate (see Rombouts, 1972;Rombouts & Pilnik, 1972;Fogarty & Ward, 1974

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Section: Discussionmentioning

confidence: 99%

Pectic Enzymes of Pigmented Strains of Clostridium

Lund¹,

Brocklehurst²

1978

Journal of General Microbiology

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“…Endopolygalacturonases are secreted by a wide variety of plant pathogens (2,5). These are the first detectable enzymes secreted by C. lindemuthianum (9) the purified C. lindemuthianum endopolygalacturonase.…”

Section: Discussionmentioning

confidence: 99%

“…evidence that polygalacturonic acid-degrading enzymes are probably able, without assistance, to degrade cell walls comes from numerous efforts to demonstrate that these enzymes macerate plant tissues (2,4,5,7,12,18,20). That polygalacturonic acid-degrading enzymes are able to attack some plant cell components.…”

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confidence: 99%

A Cell Wall-degrading Endopolygalacturonase Secreted by Colletotrichum lindemuthianum

et al. 1972

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Cultures of Colletotrichum lindertmuthianum (Saccardo and Magnus) Scribner have been induced to secrete an endopolygalacturonase (polygalacturonide glyeanohydrolase EC3.2. 1.15). This enzyme has been brought to a high state of purity bv ion exchange, gel filtration, and agarose affinity chromatography. The enzyme has optimal activity at pH 5, has an apparent molecular weight as determined bv gel filtration of about 70,000, and prefers polygalacturonic acid to pectin as its substrate. The enzymne, while hydrolyzing only 1% of the glycosidic bonds, reduces the viscosity of a polygalacturonic solution by 50 %. Nevertheless, the initial as well as the final products of polygalacturonic acid hydrolysis are predominantly tri-and digalacturonic acid and, to a lesser extent, monogalacturonic acid. The purified enzyme catalyzes the removal of about 80% of the galacturonic acid residues of cell walls isolated from suspension-cultured sycamore cells (Acer pseudoplatanus) as well as from the walls isolated from 8-day-old Red Kidney bean (Phaseolus vulgaris) hypocotvls.Most polysaccharide-degrading enzymes are unable to attack effectively their substrates within isolated cell walls. Evidence has been presented which suggests that the "wall-modifying enzyme" purified from the culture filtrate of Aspergillus niger is a polygalacturonic acid-degrading enzyme (13). Treatment of walls with the wall-modifying enzyme permits other enzymes to degrade their substrates within the wall. Additional evidence that polygalacturonic acid-degrading enzymes are probably able, without assistance, to degrade cell walls comes from numerous efforts to demonstrate that these enzymes macerate plant tissues (2,4,5,7,12,18,20

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“…The role of pectolytic enzymes in the pathogenicity of fungi and bacteria towards higher plants has been reviewed by Wood (1960) and by Bateman & Millar (1966). Pectolytic enzymes are believed to be involved in the brown rots of plant tissues caused by three species of the genus Sclerotinia.…”

Section: Introductionmentioning

confidence: 99%

The Partial Purification and Properties of Endopolygalacturonase and -L-Arabinofuranosidase secreted by Sclerotinia fructigena

Fielding

Byrde

1969

Journal of General Microbiology

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An endopolygalacturonase (PG) and an a-L-arabinofuranosidase (AF) in culture filtrates of the fungus Sclerotinia fructigena were partially purified by ion-exchange chromatography on CM-Sephadex and Ecteola-cellulose columns, and characterized. Molecular weight estimations by gel-filtration and electrophoresis on cellulose acetate strips indicated that both enzymes existed in multiple forms. The PG showed unusual stability to extreme pH values, to classical inhibitors, and to proteolytic enzymes; in the crude filtrate a bimodal temperature/stability curve was obtained.

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Pectic Enzymes in Tissue Degradation

Cited by 301 publications

References 40 publications

Pectic Enzymes of Pigmented Strains of Clostridium

Pectic Enzymes of Pigmented Strains of Clostridium

A Cell Wall-degrading Endopolygalacturonase Secreted by Colletotrichum lindemuthianum

The Partial Purification and Properties of Endopolygalacturonase and -L-Arabinofuranosidase secreted by Sclerotinia fructigena

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