Purification and characterization of a thermostable endo-β-1,4-glucanase from a novel strain of Penicillium purpurogenum

Lee, Kyoung-Mi; Jeya, Marimuthu; Joo, Ah-Reum; Singh, Raushan Kumar; Kim, In-Won; Lee, Jung-Kul

doi:10.1016/j.enzmictec.2009.11.002

Cited by 41 publications

(21 citation statements)

References 37 publications

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“…Several endo-b-1,4-glucanases from Penicillium pinophilum KMJ601 [19], P. purpurogenum [22], and P. echinulatum [32] have been reported, but all of them only have the ability to hydrolyze the b-(1 ? 4) glycosidic bonds of glucan.…”

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confidence: 99%

High-level expression of a novel Penicillium endo-1,3(4)-β-d-glucanase with high specific activity in Pichia pastoris

Chen

Meng

Shi

et al. 2012

Journal of Industrial Microbiology and Biotechnology

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A novel endo-1,3(4)-β-D-glucanase gene (bgl16C1) from Penicillium pinophilum C1 was cloned and sequenced. The 945-bp full-length gene encoded a 315-residue polypeptide consisting of a putative signal peptide of 18 residues and a catalytic domain belonging to glycosyl hydrolase family 16. The deduced amino acid sequence showed the highest identity (82%) with the putative endo-1,3(4)-β-glucanase from Talaromyces stipitatus ATCC 10500 and 60% identity with the characterized β-1,3(4)-glucanase from Paecilomyces sp. FLH30. The gene was successfully overexpressed in Pichia pastoris. Recombinant Bgl16C1 constituted 95% of total secreted proteins (2.61 g l⁻¹) with activity of 28,721 U ml⁻¹ in a 15-l fermentor. The purified recombinant Bgl16C1 had higher specific activity toward barley β-glucan (12,622 U mg⁻¹) than all known glucanases and also showed activity against lichenan and laminarin. The enzyme was optimally active at pH 5.0 and 55°C and exhibited good stability over a broad acid and alkaline pH range (>85% activity at pH 3.0-7.0 and even 30% at pH 11.0). All these favorable enzymatic properties make it attractive for potential applications in various industries.

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confidence: 99%

High-level expression of a novel Penicillium endo-1,3(4)-β-d-glucanase with high specific activity in Pichia pastoris

Chen

Meng

Shi

et al. 2012

Journal of Industrial Microbiology and Biotechnology

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“…Previous studies have reported highest activity at 60°C, such as EGa from Penicillium occitanis (Chaabouni et al 2005) and EG3 from Aspergillus fumigatus (Liu et al 2011). Similarly, numerous studies have described CMCases more active at 70°C, for example in Penicillium purpurogenum KJS506 (Lee et al 2010), Thermoascus aurantiacus (Parry et al 2002, Dave et al 2014, Daldinia eschscholzii (Karnchanatat et al 2008) and Penicillium brasilianum (Krogh et al 2009). Optimum activity at pH 5.0 was reported for CMCases from Thermomonospora sp.…”

Section: Effect Of Metal Ions and Edta On Cmcase Activity And Determimentioning

confidence: 99%

“…Cb-cel was also more thermostable than the recombinant endoglucanases ApCel5A (from Aureobasidium pullulans), GtCel12A (from Gloeophyllum trabeum) and StCel5A (from the thermophilic fungus Sporotrichum thermophile), which all presented a half-life of 2 hours at 45°C, 50°C and 55°C, respectively (Tambor et al 2012). Lee et al (2010) reported that CMCase from Penicillium purpurogenum showed a half-life of 72h, 48h, 7h and 2h at 40, 50, 60 and 70°C, respectively. Since Cb-Cel was partially purified, it is likely there are stabilizing factors enhancing its thermostability.…”

Section: Effect Of Metal Ions and Edta On Cmcase Activity And Determimentioning

confidence: 99%

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Cellulose-degrading enzyme production by Clonostachys byssicola: Partial purification and characterization of an endoglucanase

Sciuto¹

2017

Mycosphere

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Agro-industrial wastes offer potential as renewable carbon sources for microbial growth and industrial enzyme production, with potential applications in textile and biofuel industries, among others. The filamentous fungus Clonostachys byssicola was cultivated for seven days in liquid medium containing 1% (w/v) soybean hulls as unique carbon source. Hemicellulase, cellulase and pectinase activities were observed in the crude extract after seven days growth. A CMCase, denominated Cb-Cel, was partially purified using ultrafiltration and chromatographic methods. With a molecular weight of 48 kDa, the enzyme was most active at 70°C and pH 5.0, and thermostable at 40 and 50°C. Cb-Cel showed K m and V max values of 15.81 ± 1.65 mg/mL and 0.59 ± 0.03 IU/mL, respectively. Phenolic compounds (tannic, 4-hydroxybenzoic, ferulic, ρ-coumaric, cinnamic acids and vanillin) had no inhibitory or deactivator effects on enzymatic activity when tested on the concentrated fraction or Cb-Cel. Enzymatic hydrolysis of CMC and filter paper hydrolysis resulted in the release of glucose, cellopentaose and cellohexaose. Enzymatic hydrolysis of soybean hulls released mostly cellohexaose, cellopentase, mannose and xylobiose. In comparison to hydrolysis of sugarcane bagasse, the hydrolysis of soybean hulls yielded higher amounts of reducing sugars, suggesting that the enzymes secreted during growth of C. byssicola are more active on this substrate as carbon source.

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“…SDS-polyacrylamide gel electrophoresis (SDS-PAGE) is the most commonly used method for judging the apparent MW of enzymes [87][88][89]. Fungal cellulase may be of monomeric [90] or dimeric [91] in nature.…”

Section: Molecular Weight Of Fungal Cellulasesmentioning

confidence: 99%

An Overview on Fungal Cellulases with an Industrial Perspective

Sreedharan¹

2016

J Nutr Food Sci

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Lignocellulose is the most abundant biopolymer available on earth. Hydrolysis of lignocellulose into fermentable sugars, sugar acids and phenolics is the pre-requisite for its successful exploitation as substrates for the large scale production of industrially significant value added products. Though remarkable collection of lignocellulolytic microorganisms has been brought to limelight, only a few especially fungi have been studied extensively as they secrete copious lignocellulolytic enzymes extracellularly. Enzymatic hydrolysis of lignocelluloses is carried out by a group of enzymes viz., cellulases, hemicellulases, ligninases in unison or individually, and are collectively known as lignocellulolytic enzymes. In this light of this background, followed by a short introduction on lignocellulose, lignocellulolytic enzymes and mainly focused on fungal cellulase, this review discusses recent approaches on the production of cellulase by submerged and solid-state fermentation strategies; current knowledge on the purification, characterisation of cellulase; and finally concluded with detailed industrial applications of fungal cellulase.

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Purification and characterization of a thermostable endo-β-1,4-glucanase from a novel strain of Penicillium purpurogenum

Cited by 41 publications

References 37 publications

High-level expression of a novel Penicillium endo-1,3(4)-β-d-glucanase with high specific activity in Pichia pastoris

High-level expression of a novel Penicillium endo-1,3(4)-β-d-glucanase with high specific activity in Pichia pastoris

Cellulose-degrading enzyme production by Clonostachys byssicola: Partial purification and characterization of an endoglucanase

An Overview on Fungal Cellulases with an Industrial Perspective

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