Cellulosic Ethanol Production by Recombinant Cellulolytic Bacteria HarbouringpdcandadhII Genes ofZymomonas mobilis

Piriya, P. Sobana; Vasan, P. Thirumalai; Padma, V.; Vidhyadevi, U.; Archana, K. M.; Vennison, S. John

doi:10.1155/2012/817549

Cited by 18 publications

(7 citation statements)

References 28 publications

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“…Genetic engineering (recombinant) is performed on those cellulolytic bacteria and is further used in its role of converting cellulosic biomass (CMC substrate and sugarcane bagasse ) into bioethanol product more quickly and efficiently through process of fermentation at 37°C and pH 7. Cellulosic ethanol products from cellulolytic bacteria aim to reduce dependence on petroleum [ 16 ].…”

Section: Discussionmentioning

confidence: 99%

Production and assay of cellulolytic enzyme activity of Enterobacter cloacae WPL 214 isolated from bovine rumen fluid waste of Surabaya abbatoir, Indonesia

Lokapirnasari¹,

Nazar²,

Nurhajati³

et al. 2015

Vet World

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Aim:This study aims to produce and assay cellulolytic enzyme activity (endo-(1,4)-β-D-glucanase, exo-(1,4)-β-D-glucanase, and β-glucosidase, at optimum temperature and optimum pH) of Enterobacter cloacae WPL 214 isolated from bovine rumen fluid waste of Surabaya Abbatoir, Indonesia.Materials and Methods:To produce enzyme from a single colony of E. cloacae WPL 214, 98 × 1010 CFU/ml of isolates was put into 20 ml of liquid medium and incubated in a shaker incubator for 16 h at 35°C in accordance with growth time and optimum temperature of E. cloacae WPL 214. Further on, culture was centrifuged at 6000 rpm at 4°C for 15 min. Pellet was discarded while supernatant containing cellulose enzyme activity was withdrawn to assay endo-(1,4)-β-D-glucanase, exo-(1,4)-β-D-glucanase, and β-glucosidase.Results:Cellulase enzyme of E. cloacae WPL 214 isolates had endoglucanase activity of 0.09 U/ml, exoglucanase of 0.13 U/ml, and cellobiase of 0.10 U/ml at optimum temperature 35°C and optimum pH 5.Conclusion:E. cloacae WPL 214 isolated from bovine rumen fluid waste produced cellulose enzyme with activity as cellulolytic enzyme of endo-(1,4)-β-D-glucanase, exo-(1,4)-β-D-glucanase and β-glucosidase.

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Section: Discussionmentioning

confidence: 99%

Production and assay of cellulolytic enzyme activity of Enterobacter cloacae WPL 214 isolated from bovine rumen fluid waste of Surabaya abbatoir, Indonesia

Lokapirnasari¹,

Nazar²,

Nurhajati³

et al. 2015

Vet World

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“…The most established product by Z. mobilis recombinant strains is ethanol, which has been extensively investigated. In addition, ethanol production genes ( pdc and adh ) have been utilized in various other microorganisms for ethanol production, including E. coli (Piriya et al ., ). In contrast to the bioethanol derived from food‐based sugars, cellulosic bioethanol produced from lignocellulosic materials can be more economic and sustainable.…”

Section: Bioproductsmentioning

confidence: 97%

Zymomonas mobilis as a model system for production of biofuels and biochemicals

Yang

Fei

Zhang

et al. 2016

Microbial Biotechnology

172

110

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Summary Zymomonas mobilis is a natural ethanologen with many desirable industrial biocatalyst characteristics. In this review, we will discuss work to develop Z. mobilis as a model system for biofuel production from the perspectives of substrate utilization, development for industrial robustness, potential product spectrum, strain evaluation and fermentation strategies. This review also encompasses perspectives related to classical genetic tools and emerging technologies in this context.

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“…Together, the involvement of PDC and ADH2 were reported to synergistically promote growth in yeasts by glucose metabolism, as these enzymes were capable of efficiently converting intracellular pyruvate and NADH into ethanol. This event typically occurred in a homoethanol fermentation pathway, also known as the Entner-Doudoroff (ED) pathway ( Piriya et al, 2012 ). The main difference in the gene expression of ADH2 derived from S. cerevisiae and L. fermentati has been the result of ethanol.…”

Section: Resultsmentioning

confidence: 99%

Effects of glucose, ethanol and acetic acid on regulation of ADH2 gene fromLachancea fermentati

Yaacob

Ali

Salleh

et al. 2016

PeerJ

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Background. Not all yeast alcohol dehydrogenase 2 (ADH2) are repressed by glucose, as reported in Saccharomyces cerevisiae. Pichia stipitis ADH2 is regulated by oxygen instead of glucose, whereas Kluyveromyces marxianus ADH2 is regulated by neither glucose nor ethanol. For this reason, ADH2 regulation of yeasts may be species dependent, leading to a different type of expression and fermentation efficiency. Lachancea fermentati is a highly efficient ethanol producer, fast-growing cells and adapted to fermentation-related stresses such as ethanol and organic acid, but the metabolic information regarding the regulation of glucose and ethanol production is still lacking.Methods. Our investigation started with the stimulation of ADH2 activity from S. cerevisiae and L. fermentati by glucose and ethanol induction in a glucose-repressed medium. The study also embarked on the retrospective analysis of ADH2 genomic and protein level through direct sequencing and sites identification. Based on the sequence generated, we demonstrated ADH2 gene expression highlighting the conserved NAD(P)-binding domain in the context of glucose fermentation and ethanol production.Results. An increase of ADH2 activity was observed in starved L. fermentati (LfeADH2) and S. cerevisiae (SceADH2) in response to 2% (w/v) glucose induction. These suggest that in the presence of glucose, ADH2 activity was activated instead of being repressed. An induction of 0.5% (v/v) ethanol also increased LfeADH2 activity, promoting ethanol resistance, whereas accumulating acetic acid at a later stage of fermentation stimulated ADH2 activity and enhanced glucose consumption rates. The lack in upper stream activating sequence (UAS) and TATA elements hindered the possibility of Adr1 binding to LfeADH2. Transcription factors such as SP1 and RAP1 observed in LfeADH2 sequence have been implicated in the regulation of many genes including ADH2. In glucose fermentation, L. fermentati exhibited a bell-shaped ADH2 expression, showing the highest expression when glucose was depleted and ethanol-acetic acid was increased. Meanwhile, S. cerevisiae showed a constitutive ADH2 expression throughout the fermentation process.Discussion. ADH2 expression in L. fermentati may be subjected to changes in the presence of non-fermentative carbon source. The nucleotide sequence showed that ADH2 transcription could be influenced by other transcription genes of glycolysis oriented due to the lack of specific activation sites for Adr1. Our study suggests that if Adr1 is not capable of promoting LfeADH2 activation, the transcription can be controlled by Rap1 and Sp1 due to their inherent roles. Therefore in future, it is interesting to observe ADH2 gene being highly regulated by these potential transcription factors and functioned as a promoter for yeast under high volume of ethanol and organic acids.

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Cellulosic Ethanol Production by Recombinant Cellulolytic Bacteria HarbouringpdcandadhII Genes ofZymomonas mobilis

Cited by 18 publications

References 28 publications

Production and assay of cellulolytic enzyme activity of Enterobacter cloacae WPL 214 isolated from bovine rumen fluid waste of Surabaya abbatoir, Indonesia

Production and assay of cellulolytic enzyme activity of Enterobacter cloacae WPL 214 isolated from bovine rumen fluid waste of Surabaya abbatoir, Indonesia

Zymomonas mobilis as a model system for production of biofuels and biochemicals

Effects of glucose, ethanol and acetic acid on regulation of ADH2 gene fromLachancea fermentati

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