CRISPR-Cas9-mediated seb1 disruption in Talaromyces pinophilus EMU for its enhanced cellulase production

2020 ◽  
Vol 140 ◽  
pp. 109646
Author(s):  
Rupali Rahul Manglekar ◽  
Anli Geng
2018 ◽  
Vol 63 (2) ◽  
pp. 115-129
Author(s):  
Rahela Carpa ◽  
◽  
Alin Cândea ◽  
Alexei Remizovschi ◽  
Lucian Barbu-Tudoran ◽  
...  

2019 ◽  
pp. 1-3
Author(s):  
Madhuri B ◽  
Narasimha G ◽  
Balaji M*

Areca palm (ChrysalidoCarpus lutescenes) a widely used plant having feathery arching brands with 100 leaflets. All these plants produce much of waste in additions to greeny and nuts. This waste of spade is used for the production of various molecules that are used in industry and pharma sector. Fermentation techniques are used to generate economically important enzymes for industrial and pharmaceutical purposes. Cellulase enzyme degrades the cellulose in between β-1, 4 glucosidic link found in lignocellulosic complex which under physical treatment is slower to degrade. The present study of Aspergillus niger for cellulose production was carried in solid state (SS) and submerged (SM) fermentations for production of cellulase enzyme. Cellulase production in SSF after 72 h of fermentation was 8.02 and in SMF activity was 2.98 per ml of cultured broth at H 6 and temperature at 30°C. Both SMF and SSF were supplemented with lactose and lactobionic acid, which acted as cellulase P production inducers. The aim of the present work was to study the effect of Areca palm spade as substrate for Aspergillus niger and its cellulase production under SMF and SSF.


2019 ◽  
Vol 17 ◽  
Author(s):  
Farzane Kargar ◽  
Mojtaba Mortazavi ◽  
Mahmood Maleki ◽  
Masoud Torkzadeh Mahani ◽  
Younes Ghasemi ◽  
...  

Aims: The purpose of this study was to screen the bacteria producing cellulase enzymes and their bioinformatics studies. Background: Cellulose is a long-chain polymer of glucose that hydrolyzes by cellulases to glucose molecules. In order to design the new biotechnological applications, some strategies have been used as increasing the efficiency of enzyme production, generating cost-effective enzymes, producing stable enzymes and identification of new strains. Objective: On the other hand, some bacteria special features have made them suitable candidates for the identification of the new source of enzymes. In this regard, some native strains of bacteria were screened. Method: These bacteria were grown on a culture containing the liquid M9 media containing CMC to ensure the synthesis of cellulase. The formation of a clear area in the culture medium indicated decomposition of cellulose. In the following, the DNA of these bacteria were extracted and their 16S rDNA genes were amplified. Result: The results show that nine samples were able to synthesize cellulase. In following, these strains were identified using 16S rDNA. The results show that these screened bacteria belonged to the Bacillus sp., Alcaligenes sp., Alcaligenes sp., and Enterobacter sp.conclusionThe enzyme activity analysis shows that the Bacillus toyonensis, Bacillus sp. strain XA15-411 Bacillus cereus have produced the maximum yield of cellulases. However, these amounts of enzyme production in these samples are not proportional to their growth rate. As the bacterial growth chart within 4 consecutive days shows that the Alcaligenes sp. Bacillus cereus, Bacillus toyonensis, Bacillus sp. strain XA15-411 have a maximum growth rate. The study of the phylogenetic tree also shows that Bacillus species are more abundant in the production of cellulase enzyme. These bioinformatics analyses show that the Bacillus species have different evolutionary relationships and evolved in different evolutionary time. Other: However, for maximum cellulase production by this bacteria, some information as optimum temperature, optimum pH, carbon and nitrogen sources are needed for the ideal formulation of media composition. The cellulase production is closely controlled in microorganisms and the cellulase yields appear to depend on a variety of factors. However, the further studies are needed for cloning, purification and application of these new microbial cellulases in the different commercial fields as in food, detergent, and pharmaceutical, paper, textile industries and also various chemical industries. However, these novel enzymes can be further engineered through rational design or using random mutagenesis techniques.


2021 ◽  
Vol 14 (1) ◽  
Author(s):  
Jennifer A. Schmidt ◽  
Lubna V. Richter ◽  
Lisa A. Condoluci ◽  
Beth A. Ahner

Abstract Background The global demand for functional proteins is extensive, diverse, and constantly increasing. Medicine, agriculture, and industrial manufacturing all rely on high-quality proteins as major active components or process additives. Historically, these demands have been met by microbial bioreactors that are expensive to operate and maintain, prone to contamination, and relatively inflexible to changing market demands. Well-established crop cultivation techniques coupled with new advancements in genetic engineering may offer a cheaper and more versatile protein production platform. Chloroplast-engineered plants, like tobacco, have the potential to produce large quantities of high-value proteins, but often result in engineered plants with mutant phenotypes. This technology needs to be fine-tuned for commercial applications to maximize target protein yield while maintaining robust plant growth. Results Here, we show that a previously developed Nicotiana tabacum line, TetC-cel6A, can produce an industrial cellulase at levels of up to 28% of total soluble protein (TSP) with a slight dwarf phenotype but no loss in biomass. In seedlings, the dwarf phenotype is recovered by exogenous application of gibberellic acid. We also demonstrate that accumulating foreign protein represents an added burden to the plants’ metabolism that can make them more sensitive to limiting growth conditions such as low nitrogen. The biomass of nitrogen-limited TetC-cel6A plants was found to be as much as 40% lower than wildtype (WT) tobacco, although heterologous cellulase production was not greatly reduced compared to well-fertilized TetC-cel6A plants. Furthermore, cultivation at elevated carbon dioxide (1600 ppm CO2) restored biomass accumulation in TetC-cel6A plants to that of WT, while also increasing total heterologous protein yield (mg Cel6A plant−1) by 50–70%. Conclusions The work reported here demonstrates that well-fertilized tobacco plants have a substantial degree of flexibility in protein metabolism and can accommodate considerable levels of some recombinant proteins without exhibiting deleterious mutant phenotypes. Furthermore, we show that the alterations to protein expression triggered by growth at elevated CO2 can help rebalance endogenous protein expression and/or increase foreign protein production in chloroplast-engineered tobacco.


2021 ◽  
Vol 14 (1) ◽  
Author(s):  
Yumeng Chen ◽  
Xingjia Fan ◽  
Xinqing Zhao ◽  
Yaling Shen ◽  
Xiangyang Xu ◽  
...  

Abstract Background The filamentous fungus Trichoderma reesei is one of the best producers of cellulase and has been widely studied for the production of cellulosic ethanol and bio-based products. We previously reported that Mn2+ and N,N-dimethylformamide (DMF) can stimulate cellulase overexpression via Ca2+ bursts and calcium signalling in T. reesei under cellulase-inducing conditions. To further understand the regulatory networks involved in cellulase overexpression in T. reesei, we characterised the Mn2+/DMF-induced calcium signalling pathway involved in the stimulation of cellulase overexpression. Results We found that Mn2+/DMF stimulation significantly increased the intracellular levels of cAMP in an adenylate cyclase (ACY1)-dependent manner. Deletion of acy1 confirmed that cAMP is crucial for the Mn2+/DMF-stimulated cellulase overexpression in T. reesei. We further revealed that cAMP elevation induces a cytosolic Ca2+ burst, thereby initiating the Ca2+ signal transduction pathway in T. reesei, and that cAMP signalling causes the Ca2+ signalling pathway to regulate cellulase production in T. reesei. Furthermore, using a phospholipase C encoding gene plc-e deletion strain, we showed that the plc-e gene is vital for cellulase overexpression in response to stimulation by both Mn2+ and DMF, and that cAMP induces a Ca2+ burst through PLC-E. Conclusions The findings of this study reveal the presence of a signal transduction pathway in which Mn2+/DMF stimulation produces cAMP. Increase in the levels of cAMP activates the calcium signalling pathway via phospholipase C to regulate cellulase overexpression under cellulase-inducing conditions. These findings provide insights into the molecular mechanism of the cAMP–PLC–calcium signalling pathway underlying cellulase expression in T. reesei and highlight the potential applications of signal transduction in the regulation of gene expression in fungi.


2016 ◽  
Vol 27 (1) ◽  
pp. 22-35 ◽  
Author(s):  
Elsa Cherian ◽  
M. Dharmendira Kumar ◽  
G. Baskar

Purpose – The purpose of this paper is to optimize production of cellulase enzyme from agricultural waste by using Aspergillus fumigatus JCF. The study also aims at the production of bioethanol using cellulase and yeast. Design/methodology/approach – Cellulase production was carried out using modified Mandel’s medium. The optimization of the cellulase production was carried out using Plackett-Burman and Response surface methodology. Bioethanol production was carried out using simultaneous saccharification and fermentation. Findings – Maximum cellulase production at optimized conditions was found to be 2.08 IU/ml. Cellulase was used for the saccharification of three different feed stocks, i.e. sugar cane leaves, corn cob and water hyacinth. Highest amount of reducing sugar was released was 29.1 gm/l from sugarcane leaves. Sugarcane leaves produced maximum bioethanol concentration of 9.43 g/l out of the three substrates studied for bioethanol production. Originality/value – The present study reveals that by using the agricultural wastes, cellulase production can be economically increased thereby bioethanol production.


1972 ◽  
Vol 18 (10) ◽  
pp. 1543-1550 ◽  
Author(s):  
Robert G. Brown

A strain of Penicillium lilacinum, isolated from soil, produced pustulanase, β-(1 → 3)-glucanase, (EC. 3.2.1.6) and cellulase (EC.3.2.1.4) when cultivated on a medium containing pustulan as the sole source of carbon. If pustulan was replaced by ketopustulan, the production of pustulanase was stimulated about 10-fold although the amount of stimulation was dependent on the degree of oxidation of pustulan. β-(1 → 3)-Glucanase production was stimulated slightly by ketopustulan; however, the degree of oxidation did not affect significantly the yield of this enzyme. Cellulase production was either unaffected by the oxidized polymer, or at higher degrees of oxidation, decreased. Tween 80 stimulated the production of the three enzymes in media containing ketopustulan with a low degree of oxidation but was inhibitory to pustulanase and cellulase production in media containing ketopustulan with a high degree of oxidation. A combination of gel filtration and isoelectric focusing revealed that each enzyme activity was attributable to at least two proteins.


2000 ◽  
Vol 26 (5-6) ◽  
pp. 394-401 ◽  
Author(s):  
F.C. Domingues ◽  
J.A. Queiroz ◽  
J.M.S. Cabral ◽  
L.P. Fonseca

2010 ◽  
Vol 150 ◽  
pp. 169-170
Author(s):  
Yujie Zhou ◽  
Jianan Zhang ◽  
Lingmei Dai ◽  
Tiegang Hu ◽  
Dehua Liu ◽  
...  

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