Characterization of a β-1,4-glucosidase from a newly isolated strain of Pholiota adiposa and its application to the hydrolysis of biomass

Jagtap, Sujit Sadashiv; Dhiman, Saurabh Sudha; Kim, Tae Su; Li, Jinglin; Lee, Jung-Kul

doi:10.1016/j.biombioe.2013.03.032

Cited by 35 publications

(18 citation statements)

References 34 publications

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“…TthBgl had a higher acidtolerance than β-glucosidases from T. maritima MSB8 (pH 6.2) and Thermotoga petrophila RKU-1 (pH 7) (GenBank Protein No. ABQ46970) (Gabelsberger et al 1993;Haq et al 2012) but a similar optimal pH to β-glucosidase from Pholiota adiposa (Jagtap et al 2013). The optimal temperature of TthBgl was 85 ºC (Fig.…”

Section: Biochemical and Kinetic Parametersmentioning

confidence: 99%

Cloning, Purification, and Characterization of a Thermostable β-Glucosidase from Thermotoga thermarum DSM 5069

Long¹,

Shi²,

Li³

et al. 2016

BioResources

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A 56-kDa β-glucosidase (TthBgl) derived from Thermotoga thermarum DSM 5069 was expressed and purified from Escherichia coli BL21 (DE3). The purified enzyme showed hydrolytic activity towards only pnitrophenyl-β-D-glucopyranoside among the synthetic glycosides tested. The pH maximum was 5.0, and under the conditions tested, maximal activity was at 85 ºC, and pH stability occurred from 5.0 to 6.0. After being incubated at 80 ºC for 120 min, TthBgl retained 80% of its original activity. The β-glucosidase had no apparent requirement for metal ions or other co-factors, but its activity was significantly inhibited by 0.1% SDS and 1mM Cu 2+ , in which only 3% and 10% residual activity was maintained, respectively. The Vmax of TthBgl was 8.79 U mg -1 for pnitrophenyl-β-D-glucopyranoside, while the Km was 2.41 mM. The Enzyme activity was gradually inhibited by the addition of glucose, but remained approximately 50% of its original value in 500 mM glucose. 789.25 mg/L glucose was released from cellobiose by the incubation of 0.2 U/mL TthBgl for 9 h at 75 ºC. According to a phylogenetic analysis, TthBgl belongs to the glycosyl hydrolase family 3 (GH3).

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Section: Biochemical and Kinetic Parametersmentioning

confidence: 99%

Cloning, Purification, and Characterization of a Thermostable β-Glucosidase from Thermotoga thermarum DSM 5069

Long¹,

Shi²,

Li³

et al. 2016

BioResources

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“…There are more other interesting additiveeffect observations reported in literature (Kengen et al 1993;Schülein 2000;Li et al 2013;Zhao et al 2013;Jagtap et al 2013;Balasubramanian and Simões 2014).…”

Section: Chemical Additivesmentioning

confidence: 65%

“…Recently, there have been several attempts to acquire highly efficient cellulases with improved cellulolytic activity and stability (di Lauro et al 2006;Mesas et al 2012;Jagtap et al 2013). Various improvement methods including rational design and directed evolution in complementation with techniques like DNA family shuffling and error-prone polymerase chain reaction (PCR) have been prominent.…”

Section: Some Cellulase Improvement Techniquesmentioning

confidence: 99%

Lignocellulases: a review of emerging and developing enzymes, systems, and practices

Obeng

Adam

Budiman

et al. 2017

Bioresour. Bioprocess.

127

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The highly acclaimed prospect of renewable lignocellulosic biocommodities as obvious replacement of their fossilbased counterparts is burgeoning within the last few years. However, the use of the abundant lignocellulosic biomass provided by nature to produce value-added products, especially bioethanol, still faces significant challenges. One of the crucial challenging factors is in association with the expression levels, stability, and cost-effectiveness of the cellulose-degrading enzymes (cellulases). Interestingly, several recommendable endeavors in the bid to curb these challenges are in pursuance. However, the existing body of literature has not well provided the updated roadmap of the advancement and key players spearheading the current success. Moreover, the description of enzyme systems and emerging paradigms with high prospects, for example, the cell-surface display system has been ill-captured in the literature. This review focuses on the lignocellulosic biocommodity pathway, with emphasis on cellulase and hemicellulase systems. The paradigm shift towards cell-surface display system and its emerging recommendable developments have also been discussed. The attempts in supplementing cellulase with other enzymes, accessory proteins, and chemical additives have also been discussed. Moreover, some of the prominent and influential discoveries in the cellulase fraternity have been discussed.

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“…All the previous information related to enzyme production individually from Pholiota adiposa (Jagtap et al, 2013b) and Armillaria gemina was taken into account for the 6 optimized production of enzyme using a fungal consortium. Different nutritional and physical parameters that could potentially affect enzyme production were optimized using a 'onevariable-at-a-time' strategy.…”

Section: Evaluation Of Fungal Consortiamentioning

confidence: 99%

“…Similarly, the K m and V max values for the cellobiohydrolase (CBH) subunit were shown to be 5.36 mM and 18.6 U/mg-protein, respectively, with Avicel as the substrate(Jagtap et al, 2013b). On the other hand, Pholiota adiposa has been shown to be capable of producing BGL, which exhibits the highest V max for both, p-nitrophenyl glucopyranoside (pNPG) and cellobiose as substrates(Jagtap et al, 2013a).…”

mentioning

confidence: 97%

Simultaneous pretreatment and saccharification: Green technology for enhanced sugar yields from biomass using a fungal consortium

Dhiman

Haw

Kalyani

et al. 2015

Bioresource Technology

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Characterization of a β-1,4-glucosidase from a newly isolated strain of Pholiota adiposa and its application to the hydrolysis of biomass

Cited by 35 publications

References 34 publications

Cloning, Purification, and Characterization of a Thermostable β-Glucosidase from Thermotoga thermarum DSM 5069

Cloning, Purification, and Characterization of a Thermostable β-Glucosidase from Thermotoga thermarum DSM 5069

Lignocellulases: a review of emerging and developing enzymes, systems, and practices

Simultaneous pretreatment and saccharification: Green technology for enhanced sugar yields from biomass using a fungal consortium

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