Production and properties ofβ-glucosidase byNeurospora sitophila

Oguntimein, Gbekeloluwa B.; Moo‐Young, Murray

doi:10.1007/bf02310911

Cited by 15 publications

(4 citation statements)

References 25 publications

(15 reference statements)

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“…However, the decrease in CMCase activity beyond the maximum solid loading concentration, that is 5% (sugarcane bagasse and rice straw), may be due to the presence of inhibitors. This is supported by the findings of Oguntimein and Moo-Young (1991), who reported the inhibitory effect of accumulated cellobiose and cellodextrin with a low degree of polymerization [49]. Moreover, the high solid loading also increases the viscosity of the slurry, and can result in poor mixing and mass transfer problem that reduce sugar conversion [50, 51].…”

Section: Resultssupporting

confidence: 53%

Characterization of a thermophilic cellulase from Geobacillus sp. HTA426, an efficient cellulase-producer on alkali pretreated of lignocellulosic biomass

et al. 2017

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A themophilic cellulase-producing bacterium was isolated from a hot spring district and identified as Geobacillus sp. HTA426. The cellulase enzyme produced by the Geobacillus sp. HTA426 was purified through ammonium sulfate precipitation and ion exchange chromatography, with the recovery yield and fold purification of 10.14% and 5.12, respectively. The purified cellulase has a molecular weight of 40 kDa. The optimum temperature and pH for carboxymethyl cellulase (CMCase) activity of the purified cellulase were 60°C and pH 7.0, respectively. The enzyme was also stable over a wide temperature range of 50°C to 70°C after 5 h of incubation. Moreover, the strain HTA426 was able to grow and produce cellulase on alkali-treated sugarcane bagasse, rice straw and water hyacinth as carbon sources. Enzymatic hydrolysis of sugarcane bagasse, which was regarded as the most effective carbon source for cellulase production (CMCase activity = 103.67 U/mL), followed by rice straw (74.70 U/mL) and water hyacinth (51.10 U/mL). This strain producing an efficient thermostable cellulose is a potential candidate for developing a more efficient and cost-effective process for converting lignocellulosic biomass into biofuel and other industrial process.

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Section: Resultssupporting

confidence: 53%

Characterization of a thermophilic cellulase from Geobacillus sp. HTA426, an efficient cellulase-producer on alkali pretreated of lignocellulosic biomass

et al. 2017

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“…With the pre-treated CCB, at 5% solid loading rate, we attained a saccharification efficiency of 54.59% using partially purified cellulase (40 U mL −1 ) of CMCPS1 at 96 h. Cellulase, a complex of three different enzymes, acts in synergism and a cooperative association, producing substrates for each other [17,40]. The decrease in the sugar yield at low enzyme loading beyond the maximum solid loading concentration might be attributed to the presence of inhibitors, as observed earlier [41]. The accumulated cellodextrin and cellobiose with a lower degree of polymerization might inhibit hydrolysis.…”

Section: Discussionsupporting

confidence: 61%

Thermotolerant glycosyl hydrolases-producing Bacillus aerius CMCPS1 and its saccharification efficiency on HCR-laccase (LccH)-pretreated corncob biomass

Ganesan

Vinayakamoorthy

Binodh

et al. 2020

Biotechnol Biofuels

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Background: The current production of bioethanol based on lignocellulosic biomass (LCB) highly depends on thermostable enzymes and extremophiles owing to less risk of contamination. Thermophilic bacterial cellulases are preferred over fungi due to their higher growth rate, presence of complex multi-enzymes, stability, and enhanced bioconversion efficiency. Corncob, underutilized biomass, ensures energy conservation due to high lignocellulosic and more fermentable sugar content. In the present study, the thermophilic bacterium Bacillus aerius CMCPS1, isolated from the thermal springs of Manikaran, Himachal Pradesh, India, was characterized in terms of its activity, stability, and hydrolytic capacity. A two-step process comprising: (i) a combined strategy of hydrodynamic cavitation reaction (HCR)-coupled enzymatic (LccH at 6.5 U) pretreatment for delignification and (ii) subsequent hydrolysis of pre-treated (HCR-LccH) corncob biomass (CCB) using a thermostable cocktail of CMCPS1 was adopted to validate the efficiency of the process. Some of the parameters studied include lignin reduction, cellulose increase, and saccharification efficiency. Result: Among the five isolates obtained by in situ enrichment on various substrates, B. aerius CMCPS1, isolated from hot springs, exhibited the maximum hydrolytic activity of 4.11. The GH activity of the CMCPS1 strain under submerged fermentation revealed maximum filter paper activity (FPA) and endoglucanase activity of 4.36 IU mL −1 and 2.98 IU mL −1 , respectively, at 44 h. Similarly, the isolate produced exoglucanase and β-glucosidase with an activity of 1.76 IU mL −1 and 1.23 IU mL −1 at 48 h, respectively. More specifically, the enzyme endo-1,4-β-d glucanase E.C.3.2.1.4 (CMCase) produced by B. aerius CMCPS1 displayed wider stability to pH (3-9) and temperature (30-90 °C) than most fungal cellulases. Similarly, the activity of CMCase increased in the presence of organic solvents (118% at 30% acetone v/v). The partially purified CMCase from the culture supernatant of CMCPS1 registered 64% yield with twofold purification. The zymogram and SDS-PAGE analyses further confirmed the CMCase activity with an apparent molecular mass of 70 kDa. The presence of genes specific to cellulases, such as cellulose-binding domain CelB, confirmed the

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“…All results are the average of three triplicate experiments with a standard error of less than 5%. Many reports have shown the stimulatory effect of surfactants on extra-cellular enzyme production and release (Kuhad et al, 1994;Oguntimein and Moo-Young, 1991;Okeke and Obi, 1993;Maguire, 1969, 1971;Sheppard et al, 1991). It can change the hydrophobicity and zeta potential of the cell surface (Hua et al, 2003;Sheppard et al, 1991), and thus make the release of cell-bound enzyme easily.…”

Section: Use Of Surfactants For Optimizationmentioning

confidence: 99%

Effects of culture conditions and surfactants on marine lysozyme S-12 production by Bacillus sp isolated from East China sea

Zheng¹,

Sheng²,

Ji³

et al. 2013

Afr. J. Microbiol. Res.

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Effects of culture conditions and surfactants on marine lysozyme s-12 production using a statistical approach were studied in this work. Analysis of results were based on statistical calculations carried out with the one factor-at-a-time method and the L 16-orthogonal array method, using MINITAB 15.0 software. All the fermentation runs were carried out at 30±2°C on a rotary orbital shaker at 200 rpm for 24 h. The individual components selected affected the fermentation process were CaCl 2 > glucose >peptone > beef extract >MgSO 4. Furthermore, Tween 80 with 0.4 mM could enhance the production of all the extracellular proteins and S-12. The final optimized medium supported S-12 activity of 1971.25 U/mL at the end of 24 h as compared with 1095.00 U/mL before optimization.

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Production and properties ofβ-glucosidase byNeurospora sitophila

Cited by 15 publications

References 25 publications

Characterization of a thermophilic cellulase from Geobacillus sp. HTA426, an efficient cellulase-producer on alkali pretreated of lignocellulosic biomass

Characterization of a thermophilic cellulase from Geobacillus sp. HTA426, an efficient cellulase-producer on alkali pretreated of lignocellulosic biomass

Thermotolerant glycosyl hydrolases-producing Bacillus aerius CMCPS1 and its saccharification efficiency on HCR-laccase (LccH)-pretreated corncob biomass

Effects of culture conditions and surfactants on marine lysozyme S-12 production by Bacillus sp isolated from East China sea

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