Purification and Characterization of beta 1,4-Glucanases from Penicillium simplicissimum H-11

Bai, Hongzhi; Wang, Hui; Sun, Jiazeng; Irfan, Muhammad; Han, Mei; Huang, Yuan; Han, Xianpei; Yang, Qian

doi:10.15376/biores.8.3.3657-3671

Cited by 26 publications

(32 citation statements)

References 63 publications

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“…While some reports had described the purification to homogeneity of fungal b-glucosidases with high yields [11,29] apparently, an overall characteristic of this enzymes is the low recovered rate [37][38][39] and the low fold purification [40,41], suggesting its probable lability. In Penicillium italicum and Penicillium simplicissimum, an enzymatic activity recovery rate and fold purification has been reported similar to those obtained in the present study [42,43]. The enzyme purified after filtration on Sephacryl S200-HR was applied to an SDS/PAGE and the electrophoretic profile showed a single band with an estimated molecular weight of 96.8 kDa.…”

Section: Discussionsupporting

confidence: 86%

“…Fractions with b-glucosidase activity were concentrated and applied to Sephacryl S200-HR size exclusion chromatography. b-glucosidase activity was recovered in a single symmetric enzymatic activity peak (fractions [39][40][41][42][43] with an estimated M r of 197 kDa and undetectable protein measured at A 280 (Fig. 3).…”

Section: Purification Of S Schenckii B-glucosidasementioning

confidence: 97%

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Purification and characterization of an extracellular β‐glucosidase from Sporothrix schenckii

et al. 2016

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An extracellular β‐glucosidase (http://www.chem.qmul.ac.uk/iubmb/enzyme/EC3/2/1/21.html), induced by cellulose in the mycelial form of human pathogen fungus Sporothrix schenckii, was purified to homogeneity using hydroxyapatite (HAp) adsorption chromatography in batch and Sephacryl S200‐HR size exclusion chromatography. The molecular mass of the purified enzyme was estimated to be 197 kDa by size exclusion chromatography with a subunit of 96.8 kDa determined by SDS/PAGE. The β‐glucosidase exhibited optimum catalytic activity at pH 5.5/45 °C and was relatively stable for up to 24 h at 45 °C. Isoelectric focusing displayed an enzyme with a pI value of 4.0. Its activity was inhibited by Fe2+ but not by any other ions or chelating agents. Km and Vmax values of the purified enzyme were 0.012 mm and 2.56 nmol·min−1·mg−1, respectively, using 4‐methylumbelliferyl β‐D‐glucopyranoside (4‐MUG) as the substrate and 44.14 mm and 22.49 nmol·min−1·mg−1 when p‐nitrophenyl β‐D‐glucopyranoside (p‐NPG) was used. The purified β‐glucosidase was active against cellobioside, laminarin, 4‐MUG, and p‐NPG and slightly active against 4‐methylumbelliferyl β‐D‐cellobioside and p‐nitrophenyl β‐D‐cellobioside but did not hydrolyze 4‐methylumbelliferyl β‐D‐xyloside, 4‐methylumbelliferyl β‐D‐galactopyranoside nor 4‐methylumbelliferyl α‐D‐glucopyranoside. In addition, the enzyme showed transglycosylation activity when it was incubated along with different oligosaccharides. Whether the transglycosylation and cellulase activities function in vivo as a mechanism involved in the degradation of cellulolytic biomass in the saprophytic stage of S. schenckii remains to be determined.

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Section: Discussionsupporting

confidence: 86%

Section: Purification Of S Schenckii B-glucosidasementioning

confidence: 97%

Purification and characterization of an extracellular β‐glucosidase from Sporothrix schenckii

et al. 2016

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“…They suspected that the higher degradation rate of CT extract at 27°C and 37°C than at 45°C was probably related to the work of glycosidase enzyme that more active at that temperature range than at the higher temperature. However, our research did not support their claim, as the CT used in this research was steam-blanched for 6 minutes that enough to inactivate the glycoside enzyme [22,23].…”

Section: Degradation Kineticscontrasting

confidence: 59%

Thermal Degradation of Anthocyanins in Butterfly Pea (<i>Clitoria ternatea</i> L.) Flower Extract at pH 7

Marpaung¹,

Andarwulan²,

Hariyadi³

et al. 2017

AJFST

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The degradation of anthocyanins from Clitoria ternatea L. flower (CT) extract at pH 7 bottled with 0% and 50% volume of headspace (HS0 and HS50, respectively) were studied at various temperatures (7, 30, 45, 60, 75, 90°C). The extract was stable at 7°C up to 56 days. The effect of the presence of headspace to accelerate the degradation was significance at ≥30°C. The color and chemical degradation were adequately be described by the first order reaction kinetics. However, the degradation at 30°C was faster than at 45°C. The activation energy for the chemical degradation of HS0 and HS50 extracts at 45-90°C were 83.21 and 101.15 kJ/mol. The decrease of A 628 was the fastest, followed by A 580 and A 550 , respectively. By the evidence collected, it was proposed that the degradation of anthocyanins in CT extract was initiated by the unfolding and the deacylation of anionic quinonoidal base species.

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“…Singhania and Karnchanatat et al reported similar optimum pH of 5.0 for β -glucosidase from A. niger NII 08121 and Daldinia eschscholzii , respectively [36, 37]. β -glucosidases from various species of Penicillium have been reported to have optimum pH range of 4.0–6.0 [38–40]. Leite et al obtained maximum production of β -glucosidase from Thermoascus aurantiacus at pH 4.5 [41].…”

Section: Resultsmentioning

confidence: 99%

Production and Characterization of Highly Thermostableβ-Glucosidase during the Biodegradation of Methyl Cellulose byFusarium oxysporum

Olajuyigbe

Nlekerem

Ogunyewo

2016

Biochemistry Research International

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Production of β-glucosidase from Fusarium oxysporum was investigated during degradation of some cellulosic substrates (Avicel, α-cellulose, carboxymethyl cellulose (CMC), and methylcellulose). Optimized production of β-glucosidase using the cellulosic substrate that supported highest yield of enzyme was examined over 192 h fermentation period and varied pH of 3.0–11.0. The β-glucosidase produced was characterized for its suitability for industrial application. Methyl cellulose supported the highest yield of β-glucosidase (177.5 U/mg) at pH 6.0 and 30°C at 96 h of fermentation with liberation of 2.121 μmol/mL glucose. The crude enzyme had optimum activity at pH 5.0 and 70°C. The enzyme was stable over broad pH range of 4.0–7.0 with relative residual activity above 60% after 180 min of incubation. β-glucosidase demonstrated high thermostability with 83% of its original activity retained at 70°C after 180 min of incubation. The activity of β-glucosidase was enhanced by Mn2+ and Fe2+ with relative activities of 167.67% and 205.56%, respectively, at 5 mM and 360% and 315%, respectively, at 10 mM. The properties shown by β-glucosidase suggest suitability of the enzyme for industrial applications in the improvement of hydrolysis of cellulosic compounds into fermentable sugars that can be used in energy generation and biofuel production.

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Purification and Characterization of beta 1,4-Glucanases from Penicillium simplicissimum H-11

Cited by 26 publications

References 63 publications

Purification and characterization of an extracellular β‐glucosidase from Sporothrix schenckii

Purification and characterization of an extracellular β‐glucosidase from Sporothrix schenckii

Thermal Degradation of Anthocyanins in Butterfly Pea (<i>Clitoria ternatea</i> L.) Flower Extract at pH 7

Production and Characterization of Highly Thermostableβ-Glucosidase during the Biodegradation of Methyl Cellulose byFusarium oxysporum

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