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

The aim of this work was to study the production of extracellular α-amylase by Kluyveromyces marxianus IF0 0288 using optimized nutritional and cultural conditions in a complex yeast medium under aerobic batch fermentation. By applying the conventional "one-variable-at-a-time" approach and the response surface methodology, the effect of four fermentation parameters (type of carbon source, initial culture pH, temperature, and incubation time) on the growth and α-amylase production was evaluated. The production of α-amylase during 60 h of fermentation increased 13-fold under optimized conditions (1% starch, pH 6.0, 30ºC) in comparison to the conventional optimization method. The initial pH value of 6.13 and temperature of 30.3ºC were optimal conditions by the response surface methodology, leading to further improvement (up to 13-fold) in the production of extracellular α-amylase. These results constituted first evidence that K. marxianus could be potentially used as an effective source of extracellular α-amylase

Correction to: Molecular, biochemical and kinetic analysis of a novel, thermostable lipase (LipSm) from Stenotrophomonas maltophilia Psi‑1, the first member of a new bacterial lipase family (XIX)

We have recently (8th February 2018) published our article entitled “Molecular, biochemical and kinetic analysis of a novel, thermostable lipase (LipSm) from Stenotrophomonas maltophilia Psi-1, the first member of a new bacterial lipase family (XVIII)” [1]. While our manuscript was going through the final stages of publication, an article by Samoylova et al. [2] was published (12th January 2018) in the journal Extremophiles, entitled “Cloning, expression and characterization of the esterase estUT1 from Ureibacillus thermosphaericus which belongs to a new lipase family XVIII”. Since we could not have known of the work of Samoylova et al. [2] when we submitted our manuscript, and in order to avoid confusion in the scientific community, we propose to reclassify LipSm as the first characterized member of the new bacterial lipase family XIX. Therefore throughout our article [1] “lipase family XVIII” should read “lipase family XIX” (title included)

Ultrasound-assisted dilute acid hydrolysis for production of essential oils, pectin and bacterial cellulose via a citrus processing waste biorefinery

An orange peel waste biorefinery was developed employing a design of experiments approach to optimize the ultrasound-assisted dilute acid hydrolysis process applied for production of useful commodities. Central composite design-based response surface methodology was used to approximate the combined effects of process parameters in simultaneous production of essential oils, pectin and a sugar-rich hydrolyzate. Application of a desirability function determined the optimal conditions required for maximal production efficiency of essential oils, pectin and sugars as 5.75% solid loading, 1.21% acid concentration and 34.2 min duration. Maximum production yields of 0.12% w/w essential oils, 45% w/w pectin and 40% w/w sugars were achieved under optimized conditions in lab- and pilot-scale facilities. The hydrolyzate formed was applied in bacterial cellulose fermentations producing 5.82 g biopolymer per 100 g waste. Design of experiments was efficient for process analysis and optimization providing a systems platform for the study of biomass-based biorefineries

MOESM2 of Molecular, biochemical and kinetic analysis of a novel, thermostable lipase (LipSm) from Stenotrophomonas maltophilia Psi-1, the first member of a new bacterial lipase family (XVIII)

Additional file 2. Effect of metallic salts on the Michaelis–Menten parameters of LipSm