Experimental Investigation and Optimization of Process Variables Affecting the Production of Extracellular Lipase by Kluyveromyces marxianus IFO 0288

Stergiou, Panagiota‐Yiolanda; Foukis, Athanasios; Sklivaniti, Helen; Zacharaki, Paraskevi; Papagianni, Maria; Papamichael, Emmanuel M.

doi:10.1007/s12010-012-9808-3

Cited by 13 publications

(15 citation statements)

References 17 publications

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“…The expression of lipase from Candida antarctica, known as CAL-A lipase, in P. pastoris provided 0.1 g/L of lipase [28]. K.marxianus produced its own lipase with enzyme activity of 80 U/ml [8] and 0.175 U/ml [29]. The production of Thermus thermophilus esterase achieved 600 U/l activity in K. marxianus and 3000 U/l activity in K. lactis after 36 h of cultivation [25].…”

Section: Cultivation Of Mg1 and Sg1mentioning

confidence: 99%

Yeast Kluyveromyces lactis as host for expression of the bacterial lipase: cloning and adaptation of the new lipase gene from Serratia sp.

Šiekštelė

Veteikytė

Tvaska

et al. 2015

Journal of Industrial Microbiology and Biotechnology

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Many microbial lipases have been successfully expressed in yeasts, but not in industrially attractive Kluyveromyces lactis, which among other benefits can be cultivated on a medium supplemented with whey--cheap and easily available industrial waste. A new bacterial lipase from Serratia sp. was isolated and for the first time expressed into the yeast Kluyveromyces lactis by heterologous protein expression system based on a strong promoter of Kluyveromyces marxianus triosephosphate isomerase gene and signal peptide of Kluyveromyces marxianus endopolygalacturonase gene. In addition, the bacterial lipase gene was synthesized de novo by taking into account a codon usage bias optimal for K. lactis and was expressed into the yeast K. lactis also. Both resulting strains were characterized by high output level of the target protein secreted extracellularly. Secreted lipases were characterized for activity and stability.

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Section: Cultivation Of Mg1 and Sg1mentioning

confidence: 99%

Yeast Kluyveromyces lactis as host for expression of the bacterial lipase: cloning and adaptation of the new lipase gene from Serratia sp.

Šiekštelė

Veteikytė

Tvaska

et al. 2015

Journal of Industrial Microbiology and Biotechnology

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“…The strain K. marxianus (Hansen) van der Walt IFO 0288, its working stocks as well as the starting cultures, were handled and prepared as previously described (Stergiou et al 2012). All the chemicals used in this work were of analytical grade and were purchased from Sigma (U.K.), while the culture media were purchased from Lab M (U.K.).…”

Section: Strain and Reagentsmentioning

confidence: 99%

“…Cell growth and α α α α-amylase production All fermentations were performed in a stirred tank bioreactor using a standard medium supplemented with a fixed concentration of carbon source as described previously (Stergiou et al 2012). The experimental scales of the operating variables (pH and temperature) are depicted in Tables 1 and 2.…”

Section: Strain and Reagentsmentioning

confidence: 99%

“…Cell growth and α-amylase activity assays were carried out at regular intervals in aliquots of 5.0 mL which were withdrawn from the culture medium (Stergiou et al 2012). α α α α-amylase activity assays α-amylase activity was determined spectrophotometrically by monitoring the color variation of the starch-iodine complex (Ramesh and Lonsane 1989).…”

Section: Strain and Reagentsmentioning

confidence: 99%

“…The minimum and maximum ranges of variables were investigated, and all full experimental designs with respect to their values in actual and coded form, as well as the observed and predicted values of α-amylase production were obtained and listed in Tables 1 and 2. Likewise, the corresponding mathematical expressions related to the RSM approach were formulated, and empirical quartic polynomial equations of the general form of equation (1) were provided as previously described (Khuri and Cornell 1996;Singh et al 2011;Stergiou et al 2012).…”

Section: Statistical Modeling and Process Optimizationmentioning

confidence: 99%

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Optimization of the production of extracellular α-amylase by Kluyveromyces marxianus IF0 0288 by response surface methodology

Stergiou

Foukis

Theodorou

et al. 2014

Braz. arch. biol. technol.

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Bioinformatic characterization of the extracellular lipases from Kluyveromyces marxianus

Martínez-Corona

Vázquez-Marrufo

Penagos

et al. 2019

Yeast

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Lipases are hydrolytic enzymes that break the ester bonds of triglycerides, generating free fatty acids and glycerol. Extracellular lipase activity has been reported for the nonconventional yeast Kluyveromyces marxianus, grown in olive oil as a substrate, and the presence of at least eight putative lipases has been detected in its genome.However, to date, there is no experimental evidence on the physiological role of the putative lipases nor their structural and catalytic properties. In this study, a bioinformatic analysis of the genes of the putative lipases from K. marxianus L-2029 was performed, particularly identifying and characterizing the extracellular expected enzymes, due to their biotechnological relevance. The amino acid sequence of 10 putative lipases, obtained by in silico translation, ranged between 389 and 773 amino acids. Two of the analysed putative proteins showed a signal peptide, 25 and 33 amino acids long for KmYJR107Wp and KmLIP3p, and a molecular weight of 44.53 and 58.23 kDa, respectively. The amino acid alignment of KmLIP3p and KmYJR107Wp with the crystallized lipases from a patatin and the YlLip2 lipase from Yarrowia lipolytica, respectively, revealed the presence of the hydrolase characteristic motifs. From the 3D models of putative extracellular K. marxianus L-2029 lipases, the conserved pentapeptide of each was determined, being GTSMG for KmLIP3p and GHSLG for KmYJR107Wp; besides, the genes of these two enzymes (LIP3 and YJR107W) are apparently regulated by oleate response elements. The phylogenetic analysis of all K. marxianus lipases revealed evolutionary affinities with lipases from abH15.03, abH23.01, and abH23.02 families. K E Y W O R D S bioinformatic tools, Kluyveromyces marxianus, lipases, phylogeny

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Experimental Investigation and Optimization of Process Variables Affecting the Production of Extracellular Lipase by Kluyveromyces marxianus IFO 0288

Cited by 13 publications

References 17 publications

Yeast Kluyveromyces lactis as host for expression of the bacterial lipase: cloning and adaptation of the new lipase gene from Serratia sp.

Yeast Kluyveromyces lactis as host for expression of the bacterial lipase: cloning and adaptation of the new lipase gene from Serratia sp.

Optimization of the production of extracellular α-amylase by Kluyveromyces marxianus IF0 0288 by response surface methodology

Bioinformatic characterization of the extracellular lipases from Kluyveromyces marxianus

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