Enzymatic hydrolysis optimization of sweet potato (Ipomoea batatas) peel using a statistical approach

Betiku, Eriola; Akindolani, O. O.; Ismaila, A. R.

doi:10.1590/s0104-66322013000300005

Cited by 26 publications

(9 citation statements)

References 12 publications

(19 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Sweet potato peel is also a valuable source of vitamins and minerals that promote the metabolic activity of bacterium. Double fermentation approach including liquefaction and saccharification processes can also employed to improve the hydrolysis of complex structure of agro-industrial wastes using microbial enzymes (Betiku et al 2013).…”

Section: Resultsmentioning

confidence: 99%

Production of α-1,4-glucosidase from Bacillus licheniformis KIBGE-IB4 by utilizing sweet potato peel

Nawaz

Bibi

Karim

et al. 2016

Environ Sci Pollut Res

View full text Add to dashboard Cite

In the current study, sweet potato peel (Ipomoea batatas) was observed as the most favorable substrate for the maximum synthesis of α-1,4-glucosidase among various agro-industrial residues. Bacillus licheniformis KIBGE-IB4 produced 6533.0 U ml of α-1,4-glucosidase when growth medium was supplemented with 1% dried and crushed sweet potato peel. It was evident from the results that bacterial isolate secreted 6539.0 U ml of α-1,4-glucosidase in the presence of 0.4% peptone and meat extract with 0.1% yeast extract. B. licheniformis KIBGE-IB4 released 6739.0 and 7190.0 U ml of enzyme at 40 °C and pH 7.0, respectively. An improved and cost-effective growth medium design resulted 8590.0 U ml of α-1,4-glucosidase with 1.3-fold increase as compared to initial amount from B. licheniformis KIBGE-IB4. This enzyme can be used to fulfill the accelerating demand of food and pharmaceutical industries. Further purification and immobilization of this enzyme can also enhance its utility for various commercial applications. Graphical abstract Pictorial representation of maltase production from sweet potato peel.

show abstract

Section: Resultsmentioning

confidence: 99%

Production of α-1,4-glucosidase from Bacillus licheniformis KIBGE-IB4 by utilizing sweet potato peel

Nawaz

Bibi

Karim

et al. 2016

Environ Sci Pollut Res

View full text Add to dashboard Cite

show abstract

“…The dextrinized sample then allowed for saccharification, in which glucoamylase is used for further hydrolysis to produce glucose. The glucoamylase consists of a catalytic domain associated with a starch-binding molecule linked with O-glycosylated linker region that vigorously acts upon the partly treated starch molecules to release monomeric form of sugar and resulted in the formation of rough surface of the substrate as compared to the dextrinized sample (Sauer et al 2000;Betiku et al 2013). A similar kind of experiment was also conducted to digest the complex starch molecules by the action of acids and some significant starch hydrolyzing enzymes (Zhang et al 2010;de Souza et al 2019;Strąk-Graczyk and Balcerek 2020).…”

Section: Structural Property Of Treated Sprfmentioning

confidence: 99%

Optimization of saccharification prospective from starch of sweet potato roots through acid-enzyme hydrolysis: structural, chemical and elemental profiling

et al. 2021

View full text Add to dashboard Cite

The sweet potato root, a potent source of starch which is being considered as an efficient alternative for fuel ethanol production in recent times. The starchy substrate needs to be subsequently dextrinized and saccharified so as to enhance the utilization of its carbohydrates for ethanol production. In the present investigation, acid-enzyme process was conducted for the dextrinization and saccharification of sweet potato root flour (SPRF). The best optimized condition for dextrinization was achieved with an incubation period of 60 min, temperature 100 ºC and 1M HCl. However, for saccharification, the best result was obtained with an incubation of 18 h, pH 4, temperature 65 ºC and 1000 U concentration of Palkodex®. After the dextrinization process, maximum concentrations of total sugar and hydroxymethylfurfural (HMF) [380.44 ± 3.17 g/kg and 13.28 ± 0.25 mg/g, respectively] were released. Nevertheless, after saccharification, 658.80 ± 7.83 g/kg of total sugar was obtained which was about 73% more than that of dextrinization. After successful dextrinization and saccharification, the structural, chemical and elemental analysis were investigated using techniques such as scanning electron microscopy (SEM), Fourier-transforms infrared spectroscopy (FTIR) and energy-dispersive X-ray fluorescence spectrophotometer (EDXRF), respectively. Effective hydrolysis was demonstrated in thin layer chromatography (TLC) where the HCl was able to generate monomeric sugar such as glucose and maltose. On the other hand, only glucose is synthesized on the mutual effect of HCl and Palkodex®. The SEM findings indicate that the rough structure of both dextrinized and saccharified sample was gained due to the vigorous effect of both acid and enzyme subsequently. The saccharified SPRF when subjected to fermentation with Saccharomyces cerevisiae and Zymomonas mobilis separately, it was observed that Z. mobilis produced more stretching vibration of –OH than S. cerevisiae, which evidenced the better production of bioethanol. Additionally, evaluation of the influence of S. cerevisiae and Z. mobilis through elemental analysis revealed upsurge in the concentrations of S, Cl, Ca, Mn, Fe and Zn and decline in the concentrations of P, K and Cu in the fermented residue of S. cerevisiae and Z. mobilis, however, Z. mobilis showed little more variation than that of S. cerevisiae.

show abstract

“…Two methods of enzyme deactivation were evaluated. The first one was thermal shock, in which the sample was heated to the boiling point for 10 min [13,14] then cooled in an ice bath for 10 min. The second one was a change to the pH of the sample until 1.0 units with HCl 1.0M solution [12,15].…”

Section: Enzymatic Deactivationmentioning

confidence: 99%

“…At the end of each enzymatic process, the enzymes must be deactivated in order to stop the reaction. For this, there are methods such as pH deactivation, adding amounts of strong acids or bases to the sample [11,12], and temperature deactivation, in which the sample is boiled for periods between 5 and 15 min [11,13,14], or a combination of both [15].…”

Section: Introductionmentioning

confidence: 99%

Enzymatic hydrolysis of wheat starch for glucose syrup production

Acosta-Pavas

Alzate-Blandon

Colorado

2020

DYNA

View full text Add to dashboard Cite

An analysis of the enzymatic hydrolysis of wheat starch was performed. The gelatinization stage was carried out between 90-95°C for 15min. In the liquefaction stage, a commercial α-amylase was used with an enzyme-substrate ratio (E/S ratio) 0.036%w/w at 60°C and pH 5.8 for 4h. In the saccharification stage, a commercial amyloglucosidase was used with an E/S ratio of 0.11% w/w at 60°C and pH 4.3 for 6h. A second hydrolysis was evaluated using a E/S ratio of 0.18%w/w in the saccharification stage. Two methods of enzymatic deactivation, boiling temperatures and pH were evaluated. Inhibitory effects were studied by adding 180g/L of glucose to the process. It is concluded that increases in the E/S ratio decrease reaction times but reaches similar concentrations than lower ratios, the most efficient enzymatic deactivation method is pH. In the inhibition tests, it was determined that there are no glucose inhibitory effects.

show abstract

Enzymatic hydrolysis optimization of sweet potato (Ipomoea batatas) peel using a statistical approach

Cited by 26 publications

References 12 publications

Production of α-1,4-glucosidase from Bacillus licheniformis KIBGE-IB4 by utilizing sweet potato peel

Production of α-1,4-glucosidase from Bacillus licheniformis KIBGE-IB4 by utilizing sweet potato peel

Optimization of saccharification prospective from starch of sweet potato roots through acid-enzyme hydrolysis: structural, chemical and elemental profiling

Enzymatic hydrolysis of wheat starch for glucose syrup production

Contact Info

Product

Resources

About