Strain improvement of Penicillium janthinellum NCIM 1171 for increased cellulase production

Adsul, Mukund; Bastawde, K. B.; Varma, A.J.; Gokhale, D. V.

doi:10.1016/j.biortech.2006.02.036

Cited by 180 publications

(111 citation statements)

References 23 publications

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“…Classical strain development approaches have been also successful applied for improved carbohydrate-active enzyme production by fungi (Smith and Wood 1991;Antier et al 1993;Hadj-Taieb et al 2002;Adsul et al 2007). Filamentous fungi are the major producers of pectinolytic enzymes, such as polygalacturonase (PG), which are extensively used in food industry, e.g.…”

Section: Introductionmentioning

confidence: 99%

Microbial strain improvement for enhanced polygalacturonase production by Aspergillus sojae

Heerd

Tarı

Fernández‐Lahore

2014

Appl Microbiol Biotechnol

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Strain improvement is a powerful tool in commercial development of microbial fermentation processes. Strains of Aspergillus sojae which were previously identified as polygalacturonase producers were subjected to the costeffective mutagenesis and selection method, the so-called random screening. Physical (ultraviolet irradiation at 254 nm) and chemical mutagens (N-methyl-N′-nitro-Nnitrosoguanidine) were used in the development and implementation of a classical mutation and selection strategy for the improved production of pectic acid-degrading enzymes. Three mutation cycles of both mutagenic treatments and also the combination of them were performed to generate mutants descending from A. sojae ATCC 20235 and mutants of A. sojae CBS 100928. Pectinolytic enzyme production of the mutants was compared to their wild types in submerged and solid-state fermentation. Comparing both strains, higher pectinase activity was obtained by A. sojae ATCC 20235 and mutants thereof. The highest polygalacturonase activity (1,087.2±151.9 U/g) in solid-state culture was obtained by mutant M3, which was 1.7 times increased in comparison to the wild strain, A. sojae ATCC 20235. Additional, further mutation of mutant M3 for two more cycles of treatment by UV irradiation generated mutant DH56 with the highest polygalacturonase activity (98.8±8.7 U/mL) in submerged culture. This corresponded to 2.4-fold enhanced polygalacturonase production in comparison to the wild strain. The results of this study indicated the development of a classical mutation and selection strategy as a promising tool to improve pectinolytic enzyme production by both fungal strains.

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Section: Introductionmentioning

confidence: 99%

Microbial strain improvement for enhanced polygalacturonase production by Aspergillus sojae

Heerd

Tarı

Fernández‐Lahore

2014

Appl Microbiol Biotechnol

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“…Intracellular cellulase activities of both strains were significantly higher than extracellular cellulase activities, implying that Z. mobilis maintains cellulase inside cells rather than secreting it. Hence, Z. mobilis cellulase is an endoglucanase, as its highest enzyme activity was against CMC substrates (Adsul et al 2007). Several Z. mobilis strains (ATCC 39676 and CP4) natively produce endoglucanase activity against CMC (He et al bioresources.com Todhanakasem & Jittjang (2017 (Table 7) (Seo et al 2005;Kouvelis et al 2009;Kouvelis et al 2011;Pappas et al 2011;Desiniotis et al 2012;Kouvelis et al 2014).…”

Section: Resultsmentioning

confidence: 99%

Evaluation of Cellulase Production by Zymomonas mobilis

Todhanakasem

Jittjang

2016

BioResources

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Z. mobilis has been widely studied as a potential microbe for consolidated bioprocessing to convert lignocellulosic biomass to fermentable sugars while at the same time producing ethanol. To achieve this goal, Z. mobilis must be evaluated for the production of cellulolytic enzyme. This work reports on the potential of intracellular and extracellular crude extracts from Z. mobilis ZM4 and TISTR 551 to hydrolyze various cellulosic materials including carboxymethylcellulose (CMC), delignified rice bran, microcrystalline cellulose, and filter paper. Crude intracellular extracts from ZM4 and TISTR 551 showed high endoglucanase activity with CMC substrates at an optimal pH of 6 to 7 and temperature range of 30 to 40 °C. The endoglucanase activity from the crude extracts was significantly higher than the exoglucanase activity. Of the high crystalline celluloses substrates tested, the best results were obtained for the hydrolysis of delignified rice bran by crude intracellular enzyme extracts of Z. mobilis TISTR 551.

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“…The production cost of cellulase is still the major obstacle associated to hydrolysis of cellulosic materials into fermentable sugars. Therefore, improvements towards a cost effective cellulase production is essential to make this process economically viable (Adsul et al, 2007;Soccol et al, 2010;Borges et al, 2014). The cellulase complex secreted by filamentous fungi consists of three main components, endo-1,4-β-glucanase (EC 3.2.1.4), β-1,4-glucan cellobiohydrolase (EC 3.2.1.91), and β-glucosidase (EC 3.2.1.21).…”

Section: Introductionmentioning

confidence: 99%

“…Significant research efforts have been invested in evaluating and understanding the enzymatic hydrolysis of lignocellulosic substrates by cellulases produced by Trichoderma species (van Wyk and Mohulatsi, 2003;Palonen et al, 2004), which are several hundred times more active than those produced by bacteria (Adsul et al, 2007;Martins et al, 2008). Various Trichoderma strains have been extensively evaluated and implemented in processes for bioethanol production (Rosgaard et al, 2006), including studies on low cost production of cellulases using lignocellulosic residues (Kovàcz et al, 2008;Grigorevski-Lima et al, 2013).…”

Section: Introductionmentioning

confidence: 99%

“…Many traditional mutagenic strategies have been used to improve this characteristic, nevertheless, these attempts have not been totally successful yet (Chand et al, 2005;Kovàcz et al, 2008;Kovàcz et al, 2009;Jiang et al, 2011), since current enzyme production involves high costs and the production process is not yet fully defined (Adsul et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

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Production of thermophilic and acidophilic endoglucanases by mutant Trichoderma atroviride 102C1 using agro-industrial by-products

Oliveira¹,

Lima²,

Bon³

et al. 2016

Afr. J. Biotechnol.

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Many traditional mutagenic strategies have been used to improve cellulase production by microorganisms, especially fungi species. Trichoderma species are among cellulolytic fungi, those that have been most extensively studied, due to their efficient production of these enzymes. In the present study, N-methyl-N´-nitro-N-nitrosoguanidine (NTG) was used as mutagenic agent to obtain cellulolytic mutant from wild strain T. atroviride 676. After mutagenic procedures, two strains (102C1 and 104C2) were selected as promising cellulase-producing mutant. The effect of the carbon (sugarcane bagasse: SCB) and nitrogen (corn steep liquor: CSL) sources on endoglucanase production by the mutants 102C1 and 104C2 was studied using submerged cultivations at 28°C. Different concentrations of SCB and CSL were used and nine different media were generated. Mutant 102C1 showed the best results when using 2.5% SCB and 0.7% CSL. A central composite rotational design (CCRD) was performed to estimate optimal conditions of pH and temperature for endoglucanase activity of strain 102C1, which were pH 3.6 and temperature 66°C. The characterization of this acidophilic and thermophilic endoglucanase activity produced by the mutant strain 102C1 allows its use in biotechnological applications, particularly in the hydrolysis of agro industrial residues, such as SCB, for bioethanol production.

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Strain improvement of Penicillium janthinellum NCIM 1171 for increased cellulase production

Cited by 180 publications

References 23 publications

Microbial strain improvement for enhanced polygalacturonase production by Aspergillus sojae

Microbial strain improvement for enhanced polygalacturonase production by Aspergillus sojae

Evaluation of Cellulase Production by Zymomonas mobilis

Production of thermophilic and acidophilic endoglucanases by mutant Trichoderma atroviride 102C1 using agro-industrial by-products

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