Kinetics analysis of growth and lactic acid production in pH-controlled batch cultures of Lactobacillus casei KH-1 using yeast extract/corn steep liquor/glucose medium

Ha, Mi-Young; Kim, Si Wouk; Lee, Yongwoon; Kim, Myong-Jun; Kim, Seong-Jun

doi:10.1016/s1389-1723(03)90115-0

Cited by 43 publications

(25 citation statements)

References 18 publications

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“…L. casei cultivation in shake flasks has been optimized using a CCD in two blocks with temperature, yeast extract, glucose, and tryptone concentrations as the variables (38). The kinetic growth constants in pH-controlled batch cultures of this species have been studied with a CCF design (19). Experiment designs are more widely and systematically used in medical experiments concerning lactic acid bacteria and their role in the digestive tracts of mammals.…”

Section: Discussionmentioning

confidence: 99%

Metabolic Engineering of Lactobacillus plantarum for Production of l -Ribulose

Helanto¹,

Kiviharju²,

Leisola³

et al. 2007

Appl Environ Microbiol

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L-Ribulose is a rare and expensive sugar that can be used as a precursor for the production of other rare sugars of high market value such as L-ribose. In this work we describe a production process for L-ribulose using L-arabinose, a common component of polymers of lignocellulosic materials, as the starting material. A ribulokinase-deficient mutant of the heterofermentative lactic acid bacterium Lactobacillus plantarum NCIMB8826 was constructed. Expression of araA, which encodes the critical enzyme L-arabinose isomerase, was repressed by high glucose concentrations in batch cultivations. A fed-batch cultivation strategy was therefore used to maximize L-arabinose isomerase production during growth. Resting cells of the ribulokinasedeficient mutant were used for the production of L-ribulose. The isomerization of L-arabinose to L-ribulose was very unfavorable for L-ribulose formation. However, high L-ribulose yields were obtained by complexing the produced L-ribulose with borate. The process for L-ribulose production in borate buffer by resting cells was optimized using central composite designs. The experiment design suggested that the process has an optimal operation point around an L-arabinose concentration of 100 g liter ؊1 , a borate concentration of 500 mM, and a temperature of 48°C, where the statistical software predicted an initial L-ribulose production rate of 29.1 g liter ؊1 h ؊1 , a best-achievable process productivity of 14.8 g liter ؊1 h ؊1 , and a conversion of L-arabinose to L-ribulose of 0.70 mol mol ؊1 .Despite being a common metabolic intermediate in different organisms, L-ribulose is scarce in nature. This ketopentose has therefore been classified as a rare sugar (3). The markets and interest for rare and unnatural sugars have been growing, especially in the sweetener and pharmaceutical industries (40). Microbial and enzymatic reactions are very suitable for converting D sugars to various L sugars (3).Biotechnological L-ribulose production has been mainly investigated by using ribitol as the raw material. Most efficient L-ribulose production has been obtained by incubating ribitol in the presence of resting cells of acetic acid bacteria (4,14,29). The enzyme catalyzing the oxidation of ribitol to L-ribulose in these bacteria has been shown to be a membrane-bound NAD(P)-independent oxygenase (2). However, the volumes of production of ribitol are small, and it is expensive in pure form.Unlike other L sugars, L-arabinose is fairly abundant in nature. It is a common component of polymers of lignocellulosic materials (20). For example, sugar beet pulp, which is a byproduct of the sugar industry, has been reported to contain considerable amounts of L-arabinose (20%, wt/wt, of the deproteinated mass). L-Arabinose can easily be isolated from the pulp by acid or enzymatic hydrolysis, filtration, and acetone fractionation (41).The L form of ribulose is an intermediate in the pathway for L-arabinose utilization in many bacteria. The L-arabinose taken up by the cells is first isomerized to L-ribulose, which...

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Section: Discussionmentioning

confidence: 99%

Metabolic Engineering of Lactobacillus plantarum for Production of l -Ribulose

Helanto¹,

Kiviharju²,

Leisola³

et al. 2007

Appl Environ Microbiol

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“…Models of growth and lactic acid production in batch cultures of L. casei from glucose have been proposed by considering the nutrient compounds as factors in a number of designed experiments using response surface methodology. 10 Kinetic models of L. casei in continuous fermentation systems with product inhibition and glucose as substrate have also been assessed. 11,12 Another study investigated L. casei kinetics considering both product and substrate inhibition in a continuous membrane bioreactor with glucose as carbon source.…”

Section: Introductionmentioning

confidence: 99%

Kinetic modelling of lactic acid production from whey by Lactobacillus casei (NRRL B‐441)

Altıok

Tokatlı

Harsa

2006

J of Chemical Tech & Biotech

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The biomass growth, lactic acid production and lactose utilisation kinetics of lactic acid production from whey by Lactobacillus casei was studied. Batch fermentation experiments were performed at controlled pH and temperature with six different initial whey lactose concentrations (9-77 g dm −3 ) in a 3 dm 3 working volume bioreactor. Biomass growth was well described by the logistic equation with a product inhibition term. In addition, biomass and product inhibition effects were defined with corresponding power terms, which enabled adjustment of the model for low-and high-substrate conditions. The Luedeking-Piret equation defined the product formation kinetics. Substrate consumption was explained by production rate and maintenance requirements. A maximum productivity of 2.5 g dm −3 h −1 was attained with an initial lactose concentration of 35.5 g dm −3 .

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“…plantarum ATCC 14917, and Lactobacillus casei ATCC 334 were selected as representative strains for exhaustive analysis. These three species are lactic acid high-producing strains, and their lactic acid products represent three different types (D, DL, and L, respectively) (see the supplemental material for details of batch fermentation) (Table 1) (5,9,14,16,17,18,23). Moreover, both ldhL and ldhD but no lactate racemase genes or homologs were found in all three genomes during sequencing and annotation (http://www.ncbi.nlm.nih.gov/genomes/lproks.cgi).…”

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confidence: 99%