Optimization of ß-galactosidase production using Kluyveromyces lactis NRRL Y-8279 by response surface methodology

Daǧbaǧlı, Seval; Göksungur, Yekta

doi:10.2225/vol11/issue4-fulltext-12

Cited by 15 publications

(18 citation statements)

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“…Saccharomyces fragilis is described as a homothallic, hemiascomycetous yeast and production of several enzymes among them beta-galactosidase (Llorente et al, 2000;Dagbagli & Goksungur, 2008). The major common feature of S. fragilis is the capacity to assimilate lactose and to use this sugar as a carbon source.…”

Section: Introductionmentioning

confidence: 99%

“…Cell permeabilization is influenced by several operating conditions that need to be optimized. However, the traditional optimization method in which the level of one parameter is varied at a time over a certain range, while keeping the other variables constant, is generally time consuming, requiring a large number of tests (Sen & Swaminathan, 1997), and does not reflect the interaction effects among the variables and, consequently, does not depict the net effect of the various factors on the enzyme activity (Dagbagli & Goksungur, 2008). These drawbacks can be overcome by using statistical experimental factorial designs, and the experimental data of responses are usually fitted to second order polynomial functions by the response surface methodology (RSM).…”

Section: Introductionmentioning

confidence: 99%

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<b>Permeabilization of Saccharomyces fragilis IZ 275 cells with ethanol to obtain a biocatalyst with lactose hydrolysis capacity

Morioka

Colognesi

Suguimoto

2016

Acta Sci. Biol. Sci.

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The permeabilization was used to transform microorganisms in cell biocatalysts with high enzymatic activity. The Saccharomyces fragilis IZ 275 yeast cells were permeabilized with ethanol, as permeabilizing agent. To optimize the permeabilization conditions were used the design of Box-Behnken 15 trials (3 central points). The independent variables and their levels were ethanol (29, 32 and 35%), temperature (15, 20 and 25°C) and time (15, 20 and 25 min). The answer (Y) function has betagalactosidase activity (U mg-1). The optimum conditions for obtaining a high enzymatic activity were observed in 35% ethanol concentration, temperature 15ºC and 20 min. treatment time. The maximum activity of the enzyme beta-galactosidase obtained was 10.59 U mg-1. The permeabilization of the S. fragilis IZ 275 cells was efficient.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

<b>Permeabilization of Saccharomyces fragilis IZ 275 cells with ethanol to obtain a biocatalyst with lactose hydrolysis capacity

Morioka

Colognesi

Suguimoto

2016

Acta Sci. Biol. Sci.

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“…In practical terms, lactose is a rather poorly water soluble sugar, with a solubility of around 180 g/L at room temperature, so that it will tend to precipitate at lower temperatures and higher concentrations affecting the organoleptic and functional properties of products like ice-cream (Livney et al 1995), condensed sweet milk (Guu and Zall, 1991;Dagbagli and Goksungur, 2008) and "dulce de leche" (Hough et al 1990;Garitta et al 2004). Lactose is considerably less sweet than sucrose or glucose, having a sweetening power of 20 and 30% respectively (Schaafsma, 2008;Fox, 2009), so its contribution to sweetness is irrelevant and, on the contrary, it may impart an unpleasant taste to the foods containing high amounts of it (Illanes et al 1990a) and also present problems due to intolerance (Shaukat et al 2010).…”

Section: Upgrading By Enzymatic Hydrolysismentioning

confidence: 99%

“…Main interest is in the production of low or non lactose milks for lactose intolerant people (Grano et al 2004;Neuhaus et al 2006), and concentrated and frozen dairy products (Sabioni et al 1984;Lindamood et al 1989;Dagbagli and Goksungur, 2008). Hydrolysis of milk has been carried out in membrane reactors that allow the free passage of milk microsolutes (lactose and dissolved salts) to the compartment where the enzyme is, but not of its macrocomponents (proteins and fat); in this way, lactose is hydrolyzed without alteration of the remaining components of milk (Neuhaus et al 2006).…”

Section: Upgrading By Enzymatic Hydrolysismentioning

confidence: 99%

Whey upgrading by enzyme biocatalysis

Illanes¹

2011

Electro Journal of Biotech

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Whey is a co-product of processes for the production of cheese and casein that retains most of the lactose content in milk. World production of whey is estimated around 200 million tons per year with an increase rate of about 2%/per year. Milk production is seasonal, so surplus whey is unavoidable. Traditionally, whey producers have considered it as a nuisance and strategies of whey handling have been mostly oriented to their more convenient disposal. This vision has been steadily evolving because of the upgrading potential of whey major components (lactose and whey proteins), but also because of more stringent regulations of waste disposal. Only the big cheese manufacturing companies are in the position of implementing technologies for their recovery and upgrading, so there is a major challenge in incorporating medium and small size producers to a platform of whey utilization, conciliating industrial interest with environmental protection within the framework of sustainable development. Within this context, among the many technological options for whey upgrading, transformation of whey components by enzyme biocatalysis appears as prominent. In fact, enzymes are green catalysts that can perform a myriad of transformation reactions under mild conditions and with strict specificity, so reducing production costs and environmental burden. This review pretends to highlight the impact of biocatalysis within a platform of whey upgrading. Technological options are shortly reviewed and then an in-depth and critical appraisal of enzyme technologies for whey upgrading is presented, with a special focus on newly developed enzymatic processes of organic synthesis, where the added value is high, being then a powerful driving force for industrial implementation.

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“…β-galactosidase produced by these strains were measured using a quantitative β-galactosidase assay and normalized to the control strain. This liquid-based assay utilizes the ability of β-galactosidase to use O-nitrophenyl-alpha-D-galactopyranoside (ONPG) as a substrate to produce galactose and O-nitrophenol (ONP) that yields a yellow colour (Alamgir et al, 2008;Dagbagli and Goksungur, 2008).…”

Section: Translation Fidelity Of Target Genesmentioning

confidence: 99%

Identification of Novel Translation Related Genes in Saccharomyces Cerevisiae

Tan¹

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Translation in eukaryotic organisms is a vital process in the gene expression pathway. This process requires control and precision to generate functional proteins that mediate cell activities. Previously, a large scale screening approach identied 80 novel Saccharomyces cerevisiae's genes that appeared to aect translation delity. In this current research, four candidate genes were selected for further investigation: YGR117C, YNL122C, YJR014W and YNL040W. The deletions of these genes were investigated for their eects on translation delity using plasmids, pUKC817, pUKC818 and pUKC819, containing premature stop codons, UAA, UGA and UAG, respectively, in LacZ cassette. A GAL1 inducible plasmid was used to test translation eciency of these deletion strains. YNL040W and YJR014W were screened for genetic interactions with other translation genes. Altogether, our ndings provide evidence for the involvement of the target genes in translation. It also supports the idea that there exist other novel translation genes that need to be investigated. ii I would like to give my utmost gratitude to my supervisor Dr. Ashkan Golshani, whose support, guidance and contributions have helped me considerably throughout the research. I would also like to extend my thanks to my thesis committee member Dr. Myron Smith who have given insightful ideas for improvements of the research. Thanks to Bahram Samanfar for training and continuous technical support and encouragements in the lab. Thanks to Dr. Firoozeh Chalabian for her collaboration. I would also like to thank all the lab members who have provided constant encouragements and kindness. Thank you to my family for their support throughout my studies and to my wonderful partner, Kevin Kung, for his love, encouragements

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Optimization of ß-galactosidase production using Kluyveromyces lactis NRRL Y-8279 by response surface methodology

Cited by 15 publications

References 0 publications

<b>Permeabilization of Saccharomyces fragilis IZ 275 cells with ethanol to obtain a biocatalyst with lactose hydrolysis capacity

<b>Permeabilization of Saccharomyces fragilis IZ 275 cells with ethanol to obtain a biocatalyst with lactose hydrolysis capacity

Whey upgrading by enzyme biocatalysis

Identification of Novel Translation Related Genes in Saccharomyces Cerevisiae

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