High-level production of a thermoacidophilic β-glucosidase from Penicillium citrinum YS40-5 by solid-state fermentation with rice bran

Ng, I‐Son; Li, Chenwei; Chan, Shuang-Pi; Chir, Jiunly; Chen, Po-Ting; Tong, Chii-Gong; Yu, Su‐May; Ho, Tuan‐Hua David

doi:10.1016/j.biortech.2009.08.049

Cited by 90 publications

(45 citation statements)

References 35 publications

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“…1b, ammonium sulphate (AS) was the most effective nitrogen source for cellulases production by Penicillium chrysogenum QML-2, which was in accordance with some earlier reports about cellulases production by Neurospora crassa, Penicillium funiculosum, Chaetomium cellulolyticum, Trichoderma reesei, Aspergillus niger and Aspergillus terreus (Dogaris et al 2009;Rao et al 1995;Chahal et al 1996). However, it was reported that the organic nitrogen sources favored cellulases production by Aspergillus terreus M11 and b-glucosidase production by Penicillium citrinum YS40-5, respectively (Gao et al 2008;Ng et al 2010). Therefore the ability to utilize particular nitrogen sources to produce cellulases varied with species difference.…”

Section: Resultssupporting

confidence: 83%

Statistical optimization of cellulases production by Penicillium chrysogenum QML-2 under solid-state fermentation and primary application to chitosan hydrolysis

Zhang

Sang

2011

World J Microbiol Biotechnol

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Solid-state fermentation conditions for cellulases production by a newly isolated Penicillium chrysogenum QML-2 were investigated using statistical methods. At first, significant variables for cellulases production including (NH(4))(2)SO(4), initial pH and inoculum size were screened by using Plackett-Burman Design. Then the optimal regions of the significant variables were investigated by using the method of steepest ascent. Finally, central composite design and response surface analysis were adopted to determine the optimal values of the significant variables and investigate the combined effects of each variable's pair on cellulases production. The results showed that the optimal ranges of (NH(4))(2)SO(4) concentration, initial pH and inoculum size for three types of cellulases activities were 1.97-2.15 g, pH 4.32-4.41 and 13.3-13.7% (v/w), respectively. Using the mixture of corn stover powder and wheat bran (CSP/WB, 1/1) as carbon source, the optimization resulted in 370.15, 101.76 and 321.56 U/g for maximal endoglucanase activity, filter paper activity and β-glucosidase activity, respectively. Compared with maximum values of cellulases activities (endoglucanase activity 85.21 U/g, filter paper activity 16.62 U/g and β-glucosidase activity 67.68 U/g) obtained under unoptimized conditions, the optimization resulted in 3.34, 5.12 and 3.75 folds improvement for endoglucanase activity, filter paper activity and β-glucosidase activity, respectively. For chitosan hydrolysis, the crude cellulases had the optimal temperature of 55°C, pH of 4.4 and exhibited Michaelis constant (K (m)) value of 8.34 mg/ml and maximum velocity (V (max)) of 2.21 μmol glucosamine/min by 1 ml of the crude cellulases.

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Section: Resultssupporting

confidence: 83%

Statistical optimization of cellulases production by Penicillium chrysogenum QML-2 under solid-state fermentation and primary application to chitosan hydrolysis

Zhang

Sang

2011

World J Microbiol Biotechnol

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“…In that assays, higher wheat bran concentration caused increased cellulase and lipase activities while proteolytic enzyme secretion did not change. In light of this viewpoint, it is important to note that the FPase activities on SSF1 were higher than those reported recently for other fungal cellulases on rice straw [22,29] and oil palm trunk [1]. Kaur et al [16] also used plant residue substrate in SSF to evaluate the cellulase production of mutants derived from heterokaryotic Aspergillus strains.…”

Section: Discussionmentioning

confidence: 98%

Enhanced production of industrial enzymes in Mucoromycotina fungi during solid-state fermentation of agricultural wastes/by-products

Takó¹,

Kotogán²,

Krisch³

et al. 2015

Acta Biologica Hungarica

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Cellulolytic, lipolytic and proteolytic enzyme production of zygomycetes Mucor corticolus, Rhizomucor miehei, Gilbertella persicaria and Rhizopus niveus were investigated using agro-industrial wastes as substrates. Solid-state cultures were carried out on untreated corn residues (stalk and leaf) as single substrate (SSF1) or corn residues and wheat bran in mixed fermentation (SSF2). Rapid production of endoglucanase (CMCase) was observed with maximal activity reaching after about 48-h fermentation, while cellobiohydrolase (CBH) and β-glucosidase enzymes generally had their peak after 72-h incubation. Highest filter paper degrading (FPase), CMCase, CBH and β-glucosidase activities obtained were (U g -1 dss) 17.3, 74.1, 12.2 and 158.3, for R. miehei, G. persicaria, M. corticolus and Rh. niveus, respectively. M. corticolus proved to be the best lipolytic enzyme producer in SSF1 presenting 447.6 U g -1 dss yield, while R. miehei showed 517.7 U g -1 dss activity in SSF2. Rh. niveus exhibited significantly greater protease production than the other strains. Suc-AAPF-pNA hydrolyzing activities of this strain were 1.1 and 1.96 U g -1 dss in SSF1 and SSF2, respectively. We conclude that the used corn stalk and leaf residues could potentially be applicable as strong inducers for cellulase and lipase production by Mucoromycotina fungi.

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“…After which the gel is incubated in buffered MUG solution and then visualized under UV light using UV transilluminator. Appearance of fluorescent bands indicates the liberation of methylumbelliferone due to enzyme activity [93,154,168,169].…”

Section: Zymographymentioning

confidence: 99%

Microbial β-Glucosidases: Screening, Characterization, Cloning and Applications

Ahmed¹,

Aslam²,

Ashraf³

et al. 2017

JAEM

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Cellulose is the most abundant biomaterial in the biosphere and the major component of plant biomass.Cellulase is an enzymatic system required for conversion of renewable cellulose biomass into free sugar for subsequent use in different applications. Cellulase system mainly consists of three individual enzymes namely: endoglucanase, exoglucanase and β-glucosidases. β-Glucosidases are ubiquitous enzymes found in all living organisms with great biological significance. β-Glucosidases have also tremendous biotechnological applications such as biofuel production, beverage industry, food industry, cassava detoxification and oligosaccharides synthesis. Microbial β-glucosidases are preferred for industrial uses because of robust activity and novel properties exhibited by them. This review aims at describing the various biochemical methods used for screening and evaluating β-glucosidases activity from microbial sources. Subsequently, it generally highlights techniques used for purification of β-glucosidases. It then elaborates various biochemical and molecular properties of this valuable enzyme such as pH and temperature optima, glucose tolerance, substrate specificity, molecular weight, and multiplicity. Furthermore, it describes molecular cloning and expression of bacterial, fungal and metagenomic β-glucosidases. Finally, it highlights the potential biotechnological applications of β-glucosidases.

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High-level production of a thermoacidophilic β-glucosidase from Penicillium citrinum YS40-5 by solid-state fermentation with rice bran

Cited by 90 publications

References 35 publications

Statistical optimization of cellulases production by Penicillium chrysogenum QML-2 under solid-state fermentation and primary application to chitosan hydrolysis

Statistical optimization of cellulases production by Penicillium chrysogenum QML-2 under solid-state fermentation and primary application to chitosan hydrolysis

Enhanced production of industrial enzymes in Mucoromycotina fungi during solid-state fermentation of agricultural wastes/by-products

Microbial β-Glucosidases: Screening, Characterization, Cloning and Applications

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