Use of Zymomonas mobilis and Saccharomyces cerevisiae mixed with Kluyveromyces fragilis for improved ethanol production from Jerusalem artichoke tubers

Szambelan, Katarzyna; Nowak, J.; Czarnecki, Z.

doi:10.1023/b:bile.0000025889.25364.4b

Cited by 110 publications

(43 citation statements)

References 8 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…It showed that glucose with concentration above 150 g¨L´1 limits efficiency of bacteria of ethanol production, and over 220-230 g¨L´1 decreases total amount of produced ethanol (Figure 7). These results are consistent with the data measured by Nowak et al [33] and Szambelan et al [34]. They showed that glucose with concentration over 240 g¨L´1 inhibits the growth of cells of Z. mobilis (strain 3881).…”

Section: Screening the Ethanol Productivity Of Bacteriasupporting

confidence: 93%

Droplet Microfluidic Technique for the Study of Fermentation

et al. 2015

View full text Add to dashboard Cite

Abstract:We demonstrate a technique that uses microdroplets for culturing and selecting bacterial cultures in a model biotechnological application. We propose an assay for determination of ethanol concentration that provides increased dynamic range and is compatible with droplet microfluidic screening technologies. The assay comprises two enzymes-alcohol oxidase (AOX) and horseradish peroxidase (HRP)-and a colorimetric readout system of phenol-4-sulfonic acid (PSA) and 4-aminoantipyrine (4-AAP). The microdroplet method provides high repeatability (a relative error of measured ethanol concentration < 5%), high specificity for ethanol, low consumption of reagents and wide dynamic range (1-70 g¨L´1) compared to existing assays. We report the use of this method in a screen of ethanol generation efficiency of Zymomonas mobilis (strain 3881) against the concentration of glucose in the culture media.

show abstract

Section: Screening the Ethanol Productivity Of Bacteriasupporting

confidence: 93%

Droplet Microfluidic Technique for the Study of Fermentation

et al. 2015

View full text Add to dashboard Cite

show abstract

“…Jerusalem artichoke has been accepted as a good raw material for ethanol production, human diet and medical applications (Kaur and Gupta, 2002;Szambelan et al, 2004;Takeuchi and Nagashima, 2011;Chen et al, 2013;Jin et al, 2013), because the tuber is rich in fructose and inuline (Baldini et al, 2004;Saengthongpinit and Saijaanantakul, 2005). More importantly, Jerusalem artichoke has been utilized to exploit abandoned saline land in coastal zone in China at present due to its high salinity tolerance (Zhao et al, 2006;Xue and Liu, 2008;Long et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

Characterization of photosynthetic electron transport chain in bioenergy crop Jerusalem artichoke (Helianthus tuberosus L.) under heat stress for sustainable cultivation

Chen

Shao

et al. 2013

Industrial Crops and Products

View full text Add to dashboard Cite

a b s t r a c tIn order to explore the response of photosynthetic electron transport chain to heat stress, chlorophyll a fluorescence and modulated 820 nm reflection transients were examined in the leaves of Jerusalem artichoke (Helianthus tuberosus L.). J step was elevated at 43• C, suggesting that electron transport beyond primary quinone electron acceptor of photosystem II (Q A ) was inhibited. I step was elevated at 45• C due to the lowered plastoquinol re-oxidation rate. Significant decrease in the Q A reducing reaction centers per photosystem II (PSII) antenna chlorophyll and marked increase in relative variable fluorescence intensity at 300 s also occurred at 45• C, indicating that the electron transport chain from PSII donor side to Q A was injured. Overall, the fragment between Q A and plastoquinol is the most susceptible to heat in the electron transport chain before photosystem I (PSI). The maximal photochemical capacity of PSI was not affected by heat stress even at 48• C, and the interaction between PSII and PSI become unbalanced, when temperature rose to 45• C. At 45 • C, prolonged PSI oxidation occurred in the expanding leaves because of the inhibited electron donation from PSII, however, PSI oxidation amplitude decreased in the expanded leaves. We infer that electron transport chain of PSI acceptor side is more sensitive to heat stress than the chain before PSI in the expanded leaves. Therefore, electrons in PSI reaction center could not be efficiently drained to the downstream at high temperature, and then PSI oxidation was blocked.

show abstract

“…As it is abundantly available in nature and having fructose as its major composition, therefore it is suitable to be used as a substrate for fructo-oligosaccharides and high fructose syrup production for food, drink and pharmaceutical industries [4]. Moreover, fructose is also used as a substrate for bioethanol fermentation as renewable energy source by Saccharomyces cerevisiae and Zymomonas mobilis [5].…”

Section: Introductionmentioning

confidence: 99%

Production, Purification and Characterization of Inulinase from a Newly Isolated <i>Streptomyces</i> sp. CP01

Laowklom¹,

Chantanaphan²,

Pinphanichakarn³

2012

View full text Add to dashboard Cite

Inulinase is an enzyme catalyzing the hydrolysis of inulin, a plant reserve polysaccharide, into fructoses and fructooligosaccharides which are widely used as food additives. Here we report inulinase from a newly isolated Streptomyces as in the past decade there have been very few reports on inulinases from Streptomyces, especially purification and characterization of these enzymes. Out of 371 Streptomyces isolates, Streptomyces sp. CP01 produced highest inulinase activity of 0.50 U/ml. The enzyme activity was increased to 1.60 U/ml when CP01 was cultivated under the optimal conditions which consisted of using basal medium (Czapek's Dox) containing 1% (w/v) inulin extract from Jerusalem artichoke's root tubers and 0.7% (w/v) tryptone at pH8, shaking at 200 rpm and 28˚C for 24 h. The enzyme was purified from culture filtrate to about 67-fold purity by (NH 4 ) 2 SO 4 precipitation followed by four consecutive column chromatography steps. The purified enzyme is a single peptide with approximate molecular mass of 73 kDa as analyzed by gel filtration and 70.8 kDa as assessed by SDS-PAGE. The enzyme is optimally active at 55˚C and pH 6.0, however it still possesses more than 80% of the maximal activity at pH ranging from 5.5 to 9.0. It is stable at temperature up to 50˚C and at broad range of pH from 5.0 to 9.0 for 30 min. Its K m and V max values for inulin were 2.34 mM and 440 μmol·min -1 ·mg -1 , respectively. This enzyme has potential for industrial application as it is active at moderately high temperature and wide range of pH.

show abstract

Use of Zymomonas mobilis and Saccharomyces cerevisiae mixed with Kluyveromyces fragilis for improved ethanol production from Jerusalem artichoke tubers

Cited by 110 publications

References 8 publications

Droplet Microfluidic Technique for the Study of Fermentation

Droplet Microfluidic Technique for the Study of Fermentation

Characterization of photosynthetic electron transport chain in bioenergy crop Jerusalem artichoke (Helianthus tuberosus L.) under heat stress for sustainable cultivation

Production, Purification and Characterization of Inulinase from a Newly Isolated <i>Streptomyces</i> sp. CP01

Contact Info

Product

Resources

About

Use of Zymomonas mobilis and Saccharomyces cerevisiae mixed with Kluyveromyces fragilis for improved ethanol production from Jerusalem artichoke tubers

Cited by 110 publications

References 8 publications

Droplet Microfluidic Technique for the Study of Fermentation

Droplet Microfluidic Technique for the Study of Fermentation

Characterization of photosynthetic electron transport chain in bioenergy crop Jerusalem artichoke (Helianthus tuberosus L.) under heat stress for sustainable cultivation

Production, Purification and Characterization of Inulinase from a Newly Isolated &lt;i&gt;Streptomyces&lt;/i&gt; sp. CP01

Contact Info

Product

Resources

About

Production, Purification and Characterization of Inulinase from a Newly Isolated <i>Streptomyces</i> sp. CP01