Fermentation study of Cassava bagasse starch hydrolyzed's using INIAP 650 and INIAP 651 varieties and a strain of Lactobacillus leichmannii for the lactic acid production

Ecuador is an agricultural country, which has an actual production of starch obtained from cassava. Tuber processing residues do not have an economic impact; for example, the cassava bagasse, only used for plant fertilization and animal feeding. This project aimed to study the influence of the fermentation variables (pH and agitation), on the lactic acid production. Enzymatic hydrolysis of cassava bagasse starch for the varieties INIAP 650 and INIAP 651 was performed using α-amylase and glucoamylase. Then, glucose was fermented by Lactobacillus leichmannii ATCC 7830 strains, varying conditions such as agitation (150 rpm and absence) and pH (4.5, 5.0, and 5.5). Finally, the determination of lactic acid was performed by potentiometric and FTIR analysis. Conversions of cassava bagasse to reduced sugars were 71.66 and 85.05 % for INIAP 650 and INIAP 651 varieties. The best lactic acid concentrations were 27.62 and 33.48 g/L, obtained at pH 5.5 and agitation, for INIAP 650 and INIAP 651 varieties. Qualitative analysis conducted by FTIR spectrophotometry confirmed the presence of lactic acid in the reacted products. Lactic acid production from cassava bagasse starch could contribute to the Manabí and Esmeraldas provinces of Ecuador's economic development.

Optimization of β-galactosidase Production by Batch Cultures of Lactobacillus leichmannii 313 (ATCC 7830™)

The endoenzyme β-galactosidase (β-d-galactoside galactohydrolase; EC 3.2.1.23) has been used at industrial scales for the preparation of lactose-free milk and for the conversion of lactose to galacto-oligosaccharides (GOS) prebiotics. In this study, using Plackett–Burman (PB) design and the response surface methodology (RSM), the batch growth conditions for the production of β-galactosidase in DeMan-Rogosa-Sharpe (MRS) media have been studied and optimized for Lactobacillus leichmannii 313 (ATCC 7830™) for the first time. The incubation temperature (30 < T < 55 °C), starting pH (5.5 < pH < 7.5), and carbon source (glucose, lactose, galactose, fructose, and sucrose) were selected as the significant variables for optimization. The maximum crude β-galactosidase production (measured by specific activity) was 4.5 U/mg proteins and was obtained after 12 h of fermentation. The results of the PB design and further optimization by RSM showed that the initial pH of 7.0 and 15.29 g/L of lactose were the levels that gave the optimum observed and predicted β-galactosidase activities of 23.13 U/mg and 23.40 U/mg, respectively. Through RSM optimization, β-galactosidase production increased significantly (over five-fold) in optimized medium (23.13 U/mg), compared with unoptimized medium (4.5 U/mg). Moreover, the crude enzyme obtained was able to hydrolyze lactose and also produce galacto-oligosaccharides. Because its ability to produce β-galactosidase was significantly improved through optimization by RSM, L. leichmannii 313 can serve as a potential source of β-galactosidase for food applications at an industrial scale.