Research on pectin depolymerases in the sixties ‐ a literature review

Rombouts, F.M.; Pilnik, W.; Joslyn, M. A.

doi:10.1080/10408397209527133

Cited by 59 publications

(20 citation statements)

References 99 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…As the substrate is highly polymerized we conclude that the enzymes are of the endo-type, acting randomly on the substrate (Rombouts & PIlnik, 1972). Supporting this, low molecular weight oiigomers were absent when I to 4 9~~) of the pectate had been degraded but were present after I 2 to 23 :h breakdown.…”

Section: Discussionmentioning

confidence: 52%

“…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 The work reported here showed that when grown in potato tissue, strains of pigmented clostridia isolated from potatoes and C. aurantibutyricum NCIB I 0659 formed endopectate lyase and pectinesterase. These organisms differed in this respect from strains of C. felsineum which formed endopectate lyase, endopolygalacturonase and possibly exopolygalacturonase but no detectable pectinesterase.…”

Section: Introductionmentioning

confidence: 75%

“…Samples from reaction mixtures were suitably diluted with 0-I M-sodium acetate buffer, pH 3.7, and was measured. The concentration of unsaturated groups was calculated assuming an E~~~ of 4800 1 mol-l cm-l for unsaturated digalacturonic acid (Macmillan & Vaughn, 1964;Rombouts & Pilnik, 1972).…”

Section: Studies Of Reaction Productsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

“…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of the pigment, these clostridia have many properties in common with Clostridium felsineum (B. M. Lund & G. M. Wyatt, unpublished).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 …”

mentioning

confidence: 99%

See 4 more Smart Citations

Pectic Enzymes of Pigmented Strains of Clostridium

Lund¹,

Brocklehurst²

1978

Journal of General Microbiology

View full text Add to dashboard Cite

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

show abstract

Section: Discussionmentioning

confidence: 52%

Section: Introductionmentioning

confidence: 75%

Section: Studies Of Reaction Productsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

Pectic Enzymes of Pigmented Strains of Clostridium

Lund¹,

Brocklehurst²

1978

Journal of General Microbiology

View full text Add to dashboard Cite

show abstract

Purification and Properties of Apple Pectinesterase

Macdonald¹,

Evans²

1996

J. Sci. Food Agric.

View full text Add to dashboard Cite

Pectinesterase from apple was separated into two fractions by chromatography on Sephadex G‐75. The major pectinesterase was purified by cation‐exchange chromatography on CM‐Sephadex C‐50. It had a molecular mass of 36 kDa, and isoelectric point of about 9, similar to one of the major pectin‐esterases of lemon. The enzyme required the presence of cations for optimum activity and was completely inactive at temperatures above 75°C. Although the major pectinesterase had no effect on the cloud stability of apple juice, a fraction containing a minor pectinesterase caused cloud clarification.

show abstract

Purification, properties and heat inactivation of pectin methylesterase from apple (cv Golden Delicious)

Denès¹,

Baron²,

Drilleau³

2000

J. Sci. Food Agric.

View full text Add to dashboard Cite

Pectin methylesterase from apple (cv Golden Delicious) was extracted and purified by affinity chromatography on a CNBr‐Sepharose®‐PMEI column. A single pectin methylesterase peak was observed. Isoelectric points were higher than 9. Kinetic parameters of the enzyme were determined as Km = 0.098 mg ml−1 and Vmax = 3.86 µmol min−1 ml−1 of enzyme. The optimum pH of the enzyme was above 7.5 and its optimum temperature was 63 °C. The purified PME required the presence of NaCl for optimum activity, and the sodium chloride optimum concentration increased with decreasing pH (from 0.13 M at pH 7 to 0.75 M at pH 4). The heat stability of purified PME was investigated without and with glycerol (50%), and thermal resistance parameters (D and Z values) were calculated showing that glycerol improved the heat resistance of apple PME. © 2000 Society of Chemical Industry

show abstract

Research on pectin depolymerases in the sixties ‐ a literature review

Cited by 59 publications

References 99 publications

Pectic Enzymes of Pigmented Strains of Clostridium

Pectic Enzymes of Pigmented Strains of Clostridium

Purification and Properties of Apple Pectinesterase

Purification, properties and heat inactivation of pectin methylesterase from apple (cv Golden Delicious)

Contact Info

Product

Resources

About