Purification and partial characterization of polygalacturonase from Streptomyces lydicus

Jacob, Nicemol; Poorna, C. Asha; Prema, P.

doi:10.1016/j.biortech.2007.10.002

Cited by 54 publications

(47 citation statements)

References 14 publications

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“…The K M values of polygalacturonase from A. nainiana [14], R. pusillus [18], T. harzianum [32], A. giganteus [35], S. cerevisiae [33], N. crassa [23] and S. lydicus [44] for polygalacturonic acid at different buffers range from 0.22 to 5.0 mg•mL −1 , in agreement with the observed PGaseLg K M value. It should be said that a wide range of kinetic parameter values has been reported for polygalacturonases from various sources of microorganisms.…”

Section: Kinetic Characterizationsupporting

confidence: 85%

“…The effect of substrate protection is demonstrated by the fast deactivation of the enzyme at its optimal temperature of reaction. The results showed that assay conditions of pH and temperature are not the best conditions for stability, which is in agreement with the fact that catalytic performance (activity) and stability of pectinases are quite different aspects [44]. These observations typify the PGaseLg as a mesophilic enzyme.…”

Section: Physicochemical Characterizationsupporting

confidence: 75%

“…Moreover, the substrate pKa of polygalacturonic acid is 3.7, which requires acidic pH values. However, the optimal pH of pectinases from Streptomyces lydicus [44] and Neurospora crassa [23] was determined at 6.0 and from Acrophialophora nainiana [14] at 8.0. Acidic endopolygalacturonases are produced by Aspergillus kawachii [22], active at pH 2.0 Figure 4.…”

Section: Physicochemical Characterizationmentioning

confidence: 99%

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Characterization of an Exopolygalacturonase from Leucoagaricus gongylophorus, the Symbiotic Fungus of Atta sexdens

Adalberto¹,

Golfeto²,

Moreira³

et al. 2016

AER

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The present study aimed to purify and characterize one polygalacturonase from L. gongylophorus (PGaseLg), the symbiotic fungus of Atta sexdens. The enzyme was isolated by salting out of crude extract followed by two chromatographic steps. PGaseLG was identified with MS analysis and molecular exclusion chromatography revealed the monomeric nature of a protein with an estimated molecular weight of about 39 kDa. PGaseLg has an optimum temperature of 60˚C and optimum pH activity at 5.0. Using polygalacturonate as a substrate, the calculations of KM, Vmax and kcat were 0.65 mg•mL −1 , 1800 μmol•min −1 •mg −1 and 35.97 s −1 , respectively. The enzyme was stable for more than 3 h at 50˚C at pH 5.0; otherwise, at lower or higher pH values, the PGaseLg was less stable. The influence of several metals, EDTA and β-mercaptoethanol on enzyme activity was also determined. Thin layer chromatography (TLC) analyses indicated that PGaseLg is an exopolygalacturonase.

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Section: Kinetic Characterizationsupporting

confidence: 85%

Section: Physicochemical Characterizationsupporting

confidence: 75%

Section: Physicochemical Characterizationmentioning

confidence: 99%

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Characterization of an Exopolygalacturonase from Leucoagaricus gongylophorus, the Symbiotic Fungus of Atta sexdens

Adalberto¹,

Golfeto²,

Moreira³

et al. 2016

AER

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“…The K m values of 2.5 mg/mL and 1.63 mg/mL for PG produced by Aspergillus niger and Streptomyces lydicus have been reported (Parenicova et al 1998;Jacob et al 2008) though a wide range of K m values (0.059-4.7 mg/mL) for PGs are also reported in the literature (Jayani et al 2005). The catalytic rate constant k cat of purified PG was found to be 2.23 × 10 3 s −1 which is significantly higher than those reported in the literature with 90 s −1 and 29 s −1 for PG-1 and PG-2 from Aspergillus japonicus which are endo-PGs (Semenova et al 2003).…”

Section: Kinetic Parametersmentioning

confidence: 99%

“…The PG from Streptomyces lydicus also has been reported to be inhibited completely at 1 mM concentration by Hg 2+ (Jacob et al 2008). The enzyme activity was not significantly influenced by K 3 Fe(CN) 6 , Mg 2+ , Zn 2+ , Ca 2+ , Na + , K + , EDTA and NaN 3 .…”

Section: Metal Ions Comentioning

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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Immobilization studies of a pectinase produced by Aspergillus terreus

Vaz

Vici

Polizeli

et al. 2020

Biotech and App Biochem

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Aspergillus terreus can produce different holocellulose‐degrading enzymes when grown in sugarcane bagasse, with predominant pectinase activity. Thus, pectinase was selected for purification and immobilization studies. Ion exchange and molecular exclusion chromatography studies were performed, after which it was possible to semipurify the enzyme with a yield of 80%. The crude extract pectinase (PECEB) and the partially purified enzyme (PEC2) were immobilized on monoamino‐N‐aminoethyl (MANAE)‐agarose with pectinase activity yields of 66% and 98%, respectively. After immobilization in MANAE‐agarose, the pectinase showed higher activity at acidic pH (pH 4.0) when compared to the nonimmobilized enzyme. It was also found that after the immobilization process, there was a threefold improvement in the enzyme's thermostability. Also, it was possible to reuse the immobilized enzyme for up to five cycles of hydrolysis with effective production of reducing sugars (0.196 mg/g of substrate). The industrial application test revealed a significant decrease in the viscosity of guava juice when the immobilized enzyme was used. PECEB, immobilized on MANAE‐agarose, was the enzyme sample that generated the highest pulp viscosity reduction (approximately 47%). Although additional studies are needed for practical industrial application, the results obtained herein reveal the potential of application of immobilized pectinase in the industry.

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Purification and partial characterization of polygalacturonase from Streptomyces lydicus

Cited by 54 publications

References 14 publications

Characterization of an Exopolygalacturonase from <i>Leucoagaricus gongylophorus</i>, the Symbiotic Fungus of <i>Atta sexdens</i>

Characterization of an Exopolygalacturonase from <i>Leucoagaricus gongylophorus</i>, the Symbiotic Fungus of <i>Atta sexdens</i>

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

Immobilization studies of a pectinase produced by Aspergillus terreus

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Purification and partial characterization of polygalacturonase from Streptomyces lydicus

Cited by 54 publications

References 14 publications

Characterization of an Exopolygalacturonase from &lt;i&gt;Leucoagaricus gongylophorus&lt;/i&gt;, the Symbiotic Fungus of &lt;i&gt;Atta sexdens&lt;/i&gt;

Characterization of an Exopolygalacturonase from &lt;i&gt;Leucoagaricus gongylophorus&lt;/i&gt;, the Symbiotic Fungus of &lt;i&gt;Atta sexdens&lt;/i&gt;

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

Immobilization studies of a pectinase produced by Aspergillus terreus

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Characterization of an Exopolygalacturonase from <i>Leucoagaricus gongylophorus</i>, the Symbiotic Fungus of <i>Atta sexdens</i>

Characterization of an Exopolygalacturonase from <i>Leucoagaricus gongylophorus</i>, the Symbiotic Fungus of <i>Atta sexdens</i>