• KSBB Journal
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• v.28 no.5
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• pp.315-318
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• 2013

Ethanol fermentations were performed using separate hydrolysis and fermentation (SHF) processes with monosaccharides from pretreated seaweed, Eucheuma spinosum as the biomass. The pretreatment was carried out with 11% (w/v) seaweed slurry and 150 mM $H_2SO_4$ at $121^{\circ}C$ for 40 min. Enzyme hydrolysis after $H_2SO_4$ pretreatment was performed with Celluclast 1.5 L at $45^{\circ}C$ for 24 h. Five % active charcoal were added to hydrolysate to removed 5-hydroxy methylfurfural. Ethanol fermentation with 11% (w/v) seaweed hydrolysate was performed for 72~96 h using Kluyvermyces marxianus, Pichia stipits, Saccharomyces cervisiae and Candida tropicalis. Ethanol concentration was reached to 18 g/L by K. marxianus, 16 g/L by P. stipitis, 15 g/L by S. cerevisiae and 10 g/L by C. tropicalis, respectively. The ethanol yield from total monosugar was obtained 0.50 and ethanol productivity was obtained 0.38 g/L/h by K. marxianus.

• Journal of Microbiology and Biotechnology
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• v.17 no.5
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• pp.733-738
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• 2007

An extracellular exoinulinase($2,1-\beta-D$ fructan fructanohydrolase, EC 3.2.1.7), which catalyzes the hydrolysis of inulin into fructose and glucose, was purified 23.5-fold by ethanol precipitation, followed by Sephadex G-100 gel permeation from a cell-free extract of Kluyveromyces marxianus YS-1. The partially purified enzyme exhibited considerable activity between pH 5 to 6, with an optimum pH of 5.5, while it remained stable(100%) for 3 h at the optimum temperature of $50^{\circ}C$. $Mn^{2+}\;and\;Ca^{2+}$ produced a 2A-fold and 1.2-fold enhancement in enzyme activity, whereas $Hg^{2+}\;and\;Ag^{2+}$ completely inhibited the inulinase. A preparation of the partially purified enzyme effectively hydrolyzed inulin, sucrose, and raffinose, yet no activity was found with starch, lactose, and maltose. The enzyme preparation was then successfully used to hydrolyze pure inulin and raw inulin from Asparagus racemosus for the preparation of a high-fructose syrup. In a batch system, the exoinulinase hydrolyzed 84.8% of the pure inulin and 86.7% of the raw Asparagus racemosus inulin, where fructose represented 43.6mg/ml and 41.3mg/ml, respectively.

• Journal of the Korea Organic Resources Recycling Association
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• v.13 no.4
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• pp.100-106
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• 2005

Sugar beet stillages were used as a substrate for the production of single cell protein by the thermotolerant yeasts Candida rugosa, Kluyveromyces marxianus and C. utilis. The biomass production increased in accordance with the increase of pH-value, but protein content decreased. C. rugosa showed the highest crude protein production as 3.68g/l and C. utilis 2.9g/l, Kl. marxianus 2.30g/l, respectively. The rate of COD reduction in stillage versus crude protein production of C. rugosa showed the highest value as 0.35~0.39g/l as a good strain for single cell protein production using sugar beet stillages.

• Journal of Microbiology and Biotechnology
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• v.20 no.7
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• pp.1101-1106
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• 2010

Pulsed electric field (PEF) of 1Hz, 1.5 kV, and 1ms increased the activities of catalase and inulinase over the whole range of applied Se concentrations compared with the non-treated cultures. A significant effect of selenium concentration (in the range of 5-14 ${\mu}g/ml$) on both intra- and extracellular enzyme activities was noted. At a Se concentration of 10 ${\mu}g/ml$, the activities of intra- and extracellular inulinases and extracellular catalase in the PEF-treated cultures reached the maximum of 71 U/g d.m., 46 U/g d.m., and approx. 8 U/ml, respectively. The maximum activity of intracellular catalase of approx. 6 U/ml (with and without PEF) was recorded at 5 ${\mu}g$ Se/ml. Further increasing of selenium concentration caused a decrease in the activity of the enzymes.

• BMB Reports
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• v.36 no.5
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• pp.442-449
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• 2003

NAD(P)H quinone oxidoreductase is a ubiquitous enzyme that is known to directly reduce quinone substrates to hydroquinones by a two-electron reaction. We report the identification of NADPH quinone oxidoreductase from Kluyveromyces marxianus (KmQOR), which reduces quinone substrates directly to hydroquinones. The KmQOR gene was sequenced, expressed in Escherichia coli, purified, and characterized. The open-reading frame of the KmQOR gene consists of 1143 nucleotides, encoding a 380 amino acid polypeptide. The nucleotide sequence of the KmQOR gene was assigned to EMBL under accession number AY040868. The $M_r$ that was determined by SDS-PAGE for the protein subunit was about 42 kDa, and the molecular mass of the native KmQOR was 84 kDa, as determined by column calibration, indicating that the native protein is a homodimer. The KmQOR protein efficiently reduced 1,4-benzoquinone, whereas no activities were found for menadiones and methoxyquinones. These observations, and the result of an extended sequence analysis of known NADPH quinone oxidoreductase, suggest that KmQOR possesses a different action mechanism.

• Journal of the Korea Organic Resources Recycling Association
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• v.5 no.1
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• pp.1-13
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• 1997

The fermentative conversion of food wastes into feed was investigated by seeding of mixed inoculum YM (Youngjin Environmental co.), and thermotolerant yeast Kl. marxianus. For 6 days' fermentaion, the fermentation method of 2 days' aerobic followed by 4 days' anaerobic was better for the production of organic acids and increasing total microbial population than 6 days' continuous aerobic or anaerobic fermentation. By seeding YM, the total microbial count increased about 100 times of the control group. In addition, Kl. marxianus seeding together with YM increased total viable cell count, but did not increase yeast count significantly.

• KSBB Journal
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• v.5 no.1
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• pp.75-80
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• 1990

The investigations of specific growth rate, specific alcohol production rate, cell yield, alcohol yield of K. marxianus LG were performed according to the sugar concentrations, 50, 80, 110, 190, and 250g/l of extracted solution of Jerusalem Artichoke. The functipnal relationship between specific growth rate, specific alcohol production rate, and alcohol concentrations were devoted study to. In case of low concentration of alcohol, the fuctions were linear relationships. But in the region of high concentration of alcohol, they expressed the exponential relationships. The growth rate of K. marxianus was prohibited at higher than 50g/l of alcohol concentrations regardless of concentration of residual sugar. Cell and alcohol yield showed the maximum values around 25g/l of alcohol concentraton without being related to initial sugar concentrations.

• KSBB Journal
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• v.8 no.3
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• pp.272-281
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• 1993

State varibles were estimated for fermentations of K. marxianus under various dilution rates and dissolved oxygen concentrations. The number of elementary reaction stoichiometry with fixed coefficients was determined by singular variable decomposition. Stoichiometry with feasible physical meaning was obtained by target factor analysis. States of fermentations were estimated by linear quadratic programming. The process conditions of single cell production to maximize carbon source consumption were suggested.

• Journal of the Korea Organic Resources Recycling Association
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• v.8 no.4
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• pp.147-152
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• 2000

For the probiotic feed production from residual food waste by using the yeast Kluyveromyces marxianus, aerobic liquid fermentation was attempted at $35^{\circ}C$. After grinding finely, optimal fermentation conditions of the substrate was investigated in shaking incubator. By controlling water content yeast growth was studied at each different solid content of 5, 10 and 15% respectively. The most active growth of the yeast was shown at 10%. For the stimulation of the cell growth, mixed culture with Aspersillus oryzae was conducted in a 2 litre-jar fermenter. As the results, the yeast growth rate was increased, but the maximum viable cell count amounted was slightly higher as $3.5{\times}10^9/ml$ than single culture.

• Microbiology and Biotechnology Letters
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• v.22 no.2
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• pp.152-157
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• 1994

Inulinase of Kluyveromyces marxianus origin was produced by recombinant yeast Saccharomyces cerevisiae under the control of GAL1 promoter, to examine the expression and localization of inulinase in a repressed(galactose-free) or derepressed(galactose-containinga) medium. The inulinase gene(INU1A) was constitutively expressed at 6.7 units/ml in a repressed medium. When the cell started to utilize galactose in a derepressed medium, the INU1A gene began to be expressed, and the final expression level reached about 45 units/ml. According to be the nondenaturingPAGE analysis, inulinase produced by S. cerevisiae was found to be less glycosylated than the bakers yeast invertase. In addition, its glycosylation pattern was less heterogeneous than the K. marxianus inulinase. The supplementation of inulin or raffinose into the derepressed medium increased the cell growth rate, while the expression of INU1A was repressed. Regardless of the carbon sources examined, most of inulinase activity (more than 98%) was found in the extracellular medium, indicating excellent secretion efficiency.