The degradation of oligogalacturonides by the polygalacturonase of Bacillus polymyxa

Nagel, C. W.; Vaughn, Reese H.

doi:10.1016/0003-9861(61)90047-9

Cited by 68 publications

(24 citation statements)

References 12 publications

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“…The relative enzyme activity showed that the PG was also active even in acidic pH retaining its activity of 56% at pH 5 ( Figure 3A). Similar results of different alkaline polygalacturonase by different species of Bacillus were reported by other researchers [21][22][23][24]. Kapoor (2000) also reported that the polygalacturonase produced by Bacillus sp.…”

Section: Effect Of Ph and Temperature On Enzyme Activitysupporting

confidence: 87%

Characterization of pectin depolymerising exo polygalacturonase by Bacillus sp. HD2 isolated from the gut of Apis mellifera L.

Paudel¹,

Lin²,

Shen³

et al. 2015

Microbiol Discov

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Background: Polygalacturonase is an important pectin degrading enzyme. The western honey bee (Apis mellifera L.) collects pollens from different flowers which are rich source of pectin. The microbiota in the gut of honey bee, release polygalacturonase enzyme and help in pectin digestion. This study aims to isolate and characterize novel polygalacturonase producing bacterial strain from honey bee's gut. Methods: The bacterial strain was isolated by using pectin agar plate assay. The bacterial strain was identified on the basis of morphology and 16S rDNA sequence analysis. The enzyme assay was performed by using pectin as a substrate. Biomass of different fruits/vegetables was also used as a source of carbon during fermentation. The protein gel was run using SDS-PAGE for molecular weight determination of the polygalacturonase. Results:The bacterial strain showed the maximum growth, protein and polygalacturonase production at 72 hours of incubation. This bacterial strain was identified as new Bacillus sp. HD2. The sequence of this strain was successfully uploaded in NCBI Genbank database (Accession no. KP676929). The exo polygalacturonase produced by this strain of Bacillus was optimal at 40°C and exhibited enzyme activity in a wide range of pH from pH 5-12. The polygalacturonase production was enhanced by using yeast extract (3%) in the production medium and the enzyme activity was stimulated by Ca 2+ (2 mM) and SDS (200 mM). Biomass of apple's peel (1%) was found as an excellent source of carbon for the polygalacturonase production in fermentation medium (17.11±0.46 μmol ml

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Section: Effect Of Ph and Temperature On Enzyme Activitysupporting

confidence: 87%

Characterization of pectin depolymerising exo polygalacturonase by Bacillus sp. HD2 isolated from the gut of Apis mellifera L.

Paudel¹,

Lin²,

Shen³

et al. 2015

Microbiol Discov

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“…The enzyme was originally called pectin irans-eliminase, but the more acceptable trivial name is pectin lyase. Although the first lyases were specific for pectin, enzymes capable of degrading polygalacturonate by this mechanism were soon found, and both endo- (40,41,42) and exo- (43)(44)(45)(46)(47)(48)(49) action patterns were encountered. A classification scheme incorporating the trans elimination attack mechanism was proposed by Bateman and Millar (6).…”

Section: Pectic Enzymesmentioning

confidence: 98%

“…Endopolygalacturonate lyase has been described primarily from soft rot and food spoilage bacteria and related species, such as Bacillus polymyxa (40,41,151,152), Bacillus pumilis (153), Erwinia aroideae (47,48), Erwinia carotovora (42,154,155), Erwinia chrysanthemi (156), Pseudomonas fluorescens (157), Pseudomonas marginalis (135), and Xanthomonas campestris (158). Filamentous fungi frequently produce pectin lyase.…”

Section: Endopolygalacturonate Lyasementioning

confidence: 99%

Pectic Enzymes

Macmillan

SHEIMAN

1974

Advances in Chemistry

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Pectic substances, largely polygalacturonic acid or its methyl ester, are found in the primary cell walls of plants and in the middle lamella. Enzymes from plants, fungi, and bacteria degrade pectic substances and cause plant tissue maceration by esterase action on the methyl ester groups or by glycosidase or lyase action on the polygalacturonate chain. Numer ous enzymes are distinguished from one another by mecha nism (hydrolysis or trans elimination), specificity (pectin, polygalacturonate, oligogalacturonates, Δ4:5 unsaturated oligogalacturonates), action pattern (endo or exo), and stimu lation by cations. Pectic enzymes are used commercially in producing fruit juices and wines. Fundamental proper ties of the enzymes are discussed with reference to their applications in food processes. This review is primarily concerned with fundamental properties of the A pectic enzymes with some reference to their role in nature and to their applications in food processing. Because of the vast amount of literature in this field the reader is directed to other articles and books on the chemistry of pectic substances and the enzymes which degrade them Pectic substances are found in the tissues of higher plants where they have an important structural role. They are deposited in the primary cell wall during the early stages of growth and in the middle lamella where they act as "intercellular cement." The enzymatic breakdown of pectic substances in the middle lamella leads to plant tissue maceration. There fore the enzymes that degrade pectin are involved in natural processes such as the ripening of fruit (22, 23), abscission of leaves and plant organs (24), invasion of tissues by plant pathogens (6), and in the spoil age of fruits and vegetables ( 25, 26, 27 ). They are essential in the rapid decay of dead plant material and undoubtedly assist in recycling carbon (1-21).

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“…Insufficient material was available for detailed examination of the products but from the spray reactions and by comparison with the results of Nagel & Vaughn (1961) and Hsu & Vaughn (1 969) they could be, respectively, trigalacturonide, altered trigalacturonide, digalacturonide and two monomers. No spot corresponding to the altered digalacturonide was seen.…”

Section: Reaction Mechanismmentioning

confidence: 99%

“…The following solvents were used : A, ethyl acetate/pyridine/acetic acid/water (5: 5 : 1 : 3, by vol.) (Nagel & Vaughn, 1961); B, ethyl acetate/acetic acid/water (2: 1 : 2, by vol., upper phase); C, propan-1-ol/ethyl acetate/water (24: 13: 7, by vol. ); D, butan-2-ol/formic acid/water (7: 1 : 2, by vol.…”

Section: G S Coleman D C S a N D F O R D And S Beahonmentioning

confidence: 99%

The Degradation of Polygalacturonic Acid by Rumen Ciliate Protozoa

Coleman¹,

Sandford²,

Beahon³

1980

Microbiology

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295The depolymerase activity of cell-free extracts of nine species of rumen ciliate protozoa and two mixed protozoal preparations, grown in vivo and in vitro, towards polygalacturonic acid was examined. The highest activity was found with Eremoplastron bovis and Ostracodinium obtusum bilobum while there was none in the spined or spineless forms of Entodinium caudatum and little in Polyplastron multivesiculatum. On the basis of the rapid drop in viscosity, inhibition by EDTA and the production of u.v.-absorbing material, the enzymes from all active species were designated as endopectate lyases (EC 4 . 2 . 2 . 2 ) although some polygalacturonase may be present. Neither pectin nor polygalacturonic acid supported the survival or growth of any of the protozoal species tested. I N T R O D U C T I O NThere are several reports (e.g. Wright, 1960Wright, , 1961 ; Abou Akkada & Howard, 1961) that rumen ciliate protozoa contain pectin esterase and enzymes that depolymerize polygalacturonic acid. There is little information on the activity possessed by individual protozoal species although Mah & Hungate (1965) reported that Ophryoscolex purkynei contained polygalacturonate transeliminase (now called pectate lyase). This produced dehydrogenogalacturonyl digalacturonic acid (altered trimer) and dehydrogenogalacturonyl galacturonic acid (altered dimer) as final products and was similar to the bacterial enzyme studied by Hasegawa & Nagel (1962). The present paper records the activities against polygalacturonic acid of cell-free supernatant fluids obtained after the disruption of pure and mixed suspensions of rumen ciliates, grown in vivo and in vitro, and provides evidence that the enzymes are lyases. METHODSProtozoa. Sheep (Clun Forest wethers) containing single protozoal species were obtained by defaunation of the rumen by the method of Orpin (1977) followed by the introduction of a suspension of a single protozoal species isolated from the rumen and grown in vitro as described by Coleman (1978). Mixed rumen protozoa were taken from animals with a normal A-type population (Eadie, 1962(Eadie, , 1967. Entodinium bursa and the spined form of Entodinium caudatum were grown together in the rumen as the former would only grow in the presence of the latter and the latter only formed spines in the presence of the former. The sheep were fed once a day on hay chaff (800 g) and cats (100 g) and rumen contents were removed via a cannula 17 h after feeding. The preparation of washed suspensions of protozoa and the separation of a mixed population into fractions containing small or large protozoa were carried out as described by Coleman & Sandford (1979).Protozoa were grown in vitro as described by Coleman (1978) and harvested as described by Coleman (1969) except that mineral salt solution D [containing (g 1-I): KzHP04, 6.3; KH,P04, 5.0; NaCI, 0.65; CaCI, (dried), 0.045; MgSOl. 7H@, 0.091 was used throughout. The protozoa were finally suspended in water (for disruption) or in salt solution D (for experiments with living protozoa) when N2/...

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The degradation of oligogalacturonides by the polygalacturonase of Bacillus polymyxa

Cited by 68 publications

References 12 publications

Characterization of pectin depolymerising exo polygalacturonase by Bacillus sp. HD2 isolated from the gut of Apis mellifera L.

Characterization of pectin depolymerising exo polygalacturonase by Bacillus sp. HD2 isolated from the gut of Apis mellifera L.

Pectic Enzymes

The Degradation of Polygalacturonic Acid by Rumen Ciliate Protozoa

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