Microbial pectate lyases: characterization and enzymological properties

Payasi, Anurag; Sanwal, Rajni; Sanwal, G.G.

doi:10.1007/s11274-008-9870-8

Cited by 39 publications

(27 citation statements)

References 117 publications

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“…These are mainly degraded by a group of enzymes referred to as pectinases, which have been classified according to their mode of action and substrate preference into pectin esterases (EC 3.1.1.11), polygalacturonases (PGs; EC 3.2.1.15), pectate lyases (EC 4.2.2.2) and pectin lyases (EC 4.2.2.10) (Yadav et al 2009). Pectinases have been extensively reviewed and have potential applications in clarification of fruit juices, retting of fibre, treatment of pectic waste water, coffee and tea leaf fermentation, oil extraction and virus purifications (Jayani et al 2005;Satyanarayana & Kumar 2005;Payasi et al 2008;Pedrolli et al 2009). …”

Section: Introductionmentioning

confidence: 99%

Purification and characterization of an exo-polygalacturonase secreted by Rhizopus oryzae MTCC 1987 and its role in retting of Crotalaria juncea fibre

et al. 2012

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An acidic polygalacturonase (PG) secreted by Rhizopus oryzae MTCC-1987 in submerged fermentation condition has been purified to electrophoretic homogeneity using ammonium sulphate fractionation and anion exchange chromatography on diethylaminoethyl cellulose. The purified enzyme gave a single protein band in sodium dodecyl sulphatepolyacrylamide gel electrophoresis analysis with a molecular mass corresponding to 75.5 kDa. The Km and kcat values of the PG were 2.7 mg/mL and 2.23 × 10 3 s −1 , respectively, using citrus polygalacturonic acid as the substrate. The optimum pH of the purified PG was 5.0 and it does not loose activity appreciably if left for 24 hours in the pH range from 5.0 to 12.0. The optimum temperature of purified enzyme was 50• C and the enzyme does not loose activity below 30• C if exposed for two hours. The purified enzyme showed complete inhibition with 1 mM Ag + , Hg 2+ and KMnO4, while it was stimulated to some extent by Co 2+ . The purified PG exhibited retting of Crotalaria juncea fibre in absence of ethylenediaminetetraacetic acid.

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Section: Introductionmentioning

confidence: 99%

Purification and characterization of an exo-polygalacturonase secreted by Rhizopus oryzae MTCC 1987 and its role in retting of Crotalaria juncea fibre

et al. 2012

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“…The best-characterized PLs in terms of structure and mechanism are the pectate lyases (PL families 1, 2, 3, 9, and 10), recently reviewed by Payasi et al 12 All known pectate lyases share a common feature of high pH optimum (between pH 8 and 11.5) and depend strictly on the presence of metal ions for activity, Ca 2+ in the majority of cases, although for PL2 it seems to be a transition metal ion. 9 While many pectate lyases (PL1, PL3, and PL9) share the parallel β-helix fold also common to PL1 pectin lyases 9,13 and RG-hydrolase, 6 PL2 and PL10 have mostly α-helical architectures.…”

Section: Introductionmentioning

confidence: 99%

Structural and Biochemical Studies Elucidate the Mechanism of Rhamnogalacturonan Lyase from Aspergillus aculeatus

Jensen

Otten

Christensen

et al. 2010

Journal of Molecular Biology

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“…The kinetic parameters of the enzyme were calculated as 0.066 μmol.min -1 (V max ) and 2.51 mg.ml -1 (K m ) using Hanes-Woolf linearized plot. The K m value of the PMG was lower than any Bacillus species pectinases reported so far (17)(18)(19)(20)(21)(22)(23). Among the different ions tested, Ca 2+ , Cu 2+ , Mn 2+ and Mg 2+ stimulated the PMG activity that is in contrast with pectin lyase from B. pumilus (21).…”

Section: Discussionmentioning

confidence: 79%

“…The molecular mass was 104 kDa with a unique dimeric structure among Bacillus sp. pectinases (ranging from 25-115 kDa), but it is smaller than the only purified 140 kDa dimeric PMG from Sclerotinia sclerotiorum (16)(17)(18)(19)(20)(21)(22)(23).…”

Section: Discussionmentioning

confidence: 93%

Isolation and Partial Characterization of a Bacterial Thermostable Polymethyl Galacturonase from a Newly Isolated Bacillus sp. strain BR1390

Rastegari

Karbalaei‐Heidari

2014

Iran J Biotech

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Background: Pectinases are pectin degrading class of enzymes including polygalacturonase (PG), polymethyl galacturonase (PMG), pectate lyase (PEL), and pectin esterase (PE) that are commonly used in processes involving the degradation of plant materials, such as speeding up the extraction of fruit juices. Objectives: A highly methylated pectin degrading bacterium from soil covered with fruit waste was isolated and its extracellular pectinase as a novel polymethyl galacturonase was characterized. Materials and Methods: Pectin-degrading microorganism screening was performed using agar plates containing pectin as the sole carbon source. The biochemical studies were used to characterize the enzyme. Results: Bacterium with greater PMG activity was a Bacillus sp. based on 16S rDNA sequence analysis and named as a Bacillus sp. strain BR1390. Two steps column chromatography showed a dimeric protein with apparent molecular masses of 104 and 56 kDa, evident by gel filtration and SDS-PAGE. Substrate specificity analysis using various polygalacturonic acid compounds revealed its polymethyl galacturonase (PMG, EC 3.2.1.-) activity. Biochemical studies represent the thermophilic characteristics and reasonable pH stability of the polymethyl galacturonase when using pectin as substrate. The PMG activity significantly enhanced in the presence of most divalent cations such as Ca 2+ and Mg 2+ , but Hg 2+ and Fe 3+ served as strong inhibitor. Conclusions: Overall, regarding to have suitable activity in acidic conditions and high operational stability of the purified pectinase, the introduced PMG can be an ideal functional substitute for applications in the fruit juice industry, especially in citrus fruits extraction and clarification.

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Microbial pectate lyases: characterization and enzymological properties

Cited by 39 publications

References 117 publications

Purification and characterization of an exo-polygalacturonase secreted by Rhizopus oryzae MTCC 1987 and its role in retting of Crotalaria juncea fibre

Purification and characterization of an exo-polygalacturonase secreted by Rhizopus oryzae MTCC 1987 and its role in retting of Crotalaria juncea fibre

Structural and Biochemical Studies Elucidate the Mechanism of Rhamnogalacturonan Lyase from Aspergillus aculeatus

Isolation and Partial Characterization of a Bacterial Thermostable Polymethyl Galacturonase from a Newly Isolated Bacillus sp. strain BR1390

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