Purification and characterisation of processive-type endoglucanase and β-glucosidase from Aspergillus ochraceus MTCC 1810 through saccharification of delignified coir pith to glucose

Asha, Padmaja; Jose, Divya; Singh, I. S. Bright

doi:10.1016/j.biortech.2016.03.013

Cited by 29 publications

(19 citation statements)

References 13 publications

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“…For comparison, the ratio increased from 2.69 to 3.72 for the processive endoglucanase CHU_2103 when studied under similar conditions [ 15 ]. Furthermore, for two processive endoglucanases Cel9A and MtEG5, the ratios of soluble to insoluble products using FP as a substrate were 4.26 after 2 h of incubation and 3.91 after 1 h of incubation, respectively [ 7 , 12 ]. And for the processive endoglucanase AS-HT-CeluzA from A. ochraceus MTCC1810, the processivity ratio increased from 1.79 to 3.1 when the incubation time was prolonged from 3 h to 9 h [ 12 ].…”

Section: Resultsmentioning

confidence: 99%

“…Furthermore, for two processive endoglucanases Cel9A and MtEG5, the ratios of soluble to insoluble products using FP as a substrate were 4.26 after 2 h of incubation and 3.91 after 1 h of incubation, respectively [ 7 , 12 ]. And for the processive endoglucanase AS-HT-CeluzA from A. ochraceus MTCC1810, the processivity ratio increased from 1.79 to 3.1 when the incubation time was prolonged from 3 h to 9 h [ 12 ]. Although a higher ratio of soluble vs insoluble products was observed for endoglucanase EG1 (8.6), the incubation time was 24 h [ 13 ].…”

Section: Resultsmentioning

confidence: 99%

“…These CBMs are to be critical for the processivity of GH9 endoglucanases. Without CBMs, these enzymes act more like classical endoglucanases [ 10 – 12 ]. Only a few processive endoglucanases from the GH5 family have been identified to date.…”

Section: Introductionmentioning

confidence: 99%

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Processivity and enzymatic mechanism of a multifunctional family 5 endoglucanase from Bacillus subtilis BS-5 with potential applications in the saccharification of cellulosic substrates

Zheng

Pedroso

et al. 2018

Biotechnol Biofuels

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BackgroundPresently, enzymes still constitute a major part of the cost of biofuel production from lignocellulosic biomass. Processive endoglucanases, which possess both endoglucanase and exoglucanase activity, have the potential to reduce the costs of biomass saccharification when used together with commercial cellulases. Therefore, the exploration of new processive endoglucanases has attracted much attention with a view to accelerating the industrialization of biofuels and biochemicals.ResultsThe endoglucanase EG5C and its truncated form EG5C-1 from Bacillus subtilis BS-5 were expressed and characterized. EG5C was a typical endoglucanase, comprised of a family 5 catalytic domain and family 3 carbohydrate-binding domain, and which had high activity toward soluble cellulosic substrates, but low activity toward insoluble cellulosic substrates. Importantly, the truncated form EG5C-1 was a processive endoglucanase that hydrolyzed not only carboxymethyl cellulose (CMC), but also insoluble cellulosic substrates. The hydrolytic activities of EG5C-1 towards CMC, phosphoric acid-swollen cellulose (PASC), p-nitrophenyl-β-d-cellobioside, filter paper and Avicel are 4170, 700, 2550, 405 and 320 U/μmol, respectively. These data demonstrated that EG5C-1 had higher activity ratio of exoglucanase to endoglucanase than other known processive endoglucanases. When PASC was degraded by EG5C-1, the ratio of soluble to insoluble reducing sugars was about 3.7 after 3 h of incubation with cellobiose and cellotriose as the main products. Importantly, EG5C-1 alone was able to hydrolyze filter paper and PASC. At 5% substrate concentration and 10 FPU/g PASC enzyme loading, the saccharification yield was 76.5% after 60 h of incubation. Replacement of a phenylalanine residue (F238) by an alanine at the entrance/exit of the substrate binding cleft significantly reduces the ability of EG5C-1 to degrade filter paper and Avicel, but this mutation has little impact on CMCase activity. The processivity of this mutant was also greatly reduced while its cellulose binding ability was markedly enhanced.ConclusionsThe processive endoglucanase EG5C-1 from B. subtilis BS-5 exhibits excellent properties that render it a suitable candidate for use in biofuel and biochemical production from lignocellulosic biomass. In addition, our studies also provide useful information for research on enzyme processivity at the molecular level.Electronic supplementary materialThe online version of this article (10.1186/s13068-018-1022-2) contains supplementary material, which is available to authorized users.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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Processivity and enzymatic mechanism of a multifunctional family 5 endoglucanase from Bacillus subtilis BS-5 with potential applications in the saccharification of cellulosic substrates

Zheng

Pedroso

et al. 2018

Biotechnol Biofuels

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“…Aspergillus flavus is reported as a potential strain for cellulase production by Solid State Fermentation (SSF) using the lignocellulosic media (Sajith et al 2014). Fungi of Aspergillus, which are reported as the cellulase producers among others are A. nidulans, A. niger and A. oryzae (Jabasingh 2011; Amore and Faraco 2012), A. fumigatus (Liu et al 2011), and A. ochraceus (Asha et al 2016). Fungi of Aspergillus has been known as the enzyme producers for the production of high extracellular protein, bearing good ability in the fermentation process, and the generation of various enzymes for wood-degradation.…”

Section: Discussionmentioning

confidence: 99%

Isolation and screening of cellulolytic fungi from Salacca zalacca leaf litter

2017

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Cellulases are the main enzymes in a bioconversion of lignocellulosic biomass. Fungal cellulases have been proven to be better candidates for this process than other microbial cellulases since they secrete free cellulase complex including endoglucanases, cellobiohydrolases, and β-glucosidase. This study was conducted to isolate and screen of cellulolytic fungi from Salacca leaf litter. There were about 12 fungal isolates which were obtained in this research and 8 isolates showed cellulolytic activity. Based on morphological characters, these cellulolytic fungi were identified as belonging to 4 genera, i.e. Penicillium, Aspergillus, Paecilomyces, and Thielaviopsis. Based on clear zone formation, isolate SLL03, SLL06 and SLL10 showed highest cellulolytic activity. Whereas, based on 18S rRNA gene sequence, these isolates were identified as Aspergillums flavus (SLL03), Penicillium sp. (SLL06) Thielaviopsis ethacetica (SLL10). Therefore, these isolates would be good candidates for cellulase producer.

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“…The genus Aspergillus has potential for enzyme industry, because almost all fungi of this genus synthesize cellulase (Mai et al 2018). Production of β-glucosidase from different Aspergillus strains has been widely reported, such as Aspergillus niger (Zahoor et al 2011), Aspergillus oryzae (Watanabe et al 2016), Aspergillus terreus (Elshafei et al 2011), Aspergillus fumigatus (Cao et al 2015), Aspergillus saccharolyticus (Sørensen et al 2014), Aspergillus ochraceus (Asha et al 2016), and Aspergillus japonicus (da Silva et al 2014). The use of A. niger as a source of -glucosidase has been widely applied (Qian et al 2012).…”

Section: Introductionmentioning

confidence: 99%

Effect of growth conditions on β-glucosidase production by local isolate of Aspergillus niger using rice bran substrate

et al. 2020

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Abstract. Sugiwati S, Hanafi M, Lioe HN, Suhartono MT. 2020. Effect of growth conditions on β-glucosidase production by local isolate of Aspergillus niger using rice bran substrate. Biodiversitas 21: 4058-4066. β-Glucosidase is the family of glycosyl hydrolase that have potential role in various food industry, such as in tea, wine and vanilla industries to increase the aroma and production of isoflavone aglycons in soybean flour. The present work produced β-glucosidase from local isolate of Aspergillus niger InaCC F57 under solid-state fermentation (SSF) using rice bran substrate. Fermentation process was made in various conditions with respect to carbon source as substrate, initial pH of fermentation medium, incubation time, water to substrate ratio, fermentation temperature, and addition of Mandels mineral salts solution. The results showed that activity of β-glucosidase was best at, i.e., 2.45 U/mL, with the use of rice bran as substrate. Furthermore, optimum condition for the highest production of β-glucosidase occurred at pH 2.0, incubation time of 5 days, water to substrate ratio of 1.5: 1, and incubation temperature of 32°C. Additionally, in optimum fermentation conditions, production of β-glucosidase could be enhanced up to 26.22% with the presence of Mandels mineral salts solution as compared to the control.

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Purification and characterisation of processive-type endoglucanase and β-glucosidase from Aspergillus ochraceus MTCC 1810 through saccharification of delignified coir pith to glucose

Cited by 29 publications

References 13 publications

Processivity and enzymatic mechanism of a multifunctional family 5 endoglucanase from Bacillus subtilis BS-5 with potential applications in the saccharification of cellulosic substrates

Processivity and enzymatic mechanism of a multifunctional family 5 endoglucanase from Bacillus subtilis BS-5 with potential applications in the saccharification of cellulosic substrates

Isolation and screening of cellulolytic fungi from Salacca zalacca leaf litter

Effect of growth conditions on β-glucosidase production by local isolate of Aspergillus niger using rice bran substrate

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