scholarly journals Understanding the Effects of Lactose Hydrolysis Modeling on the Main Oligosaccharides in Goat Milk Whey Permeate

Molecules ◽  
2019 ◽  
Vol 24 (18) ◽  
pp. 3294 ◽  
Author(s):  
Caroline Thum ◽  
Valerie Weinborn ◽  
Daniela Barile ◽  
Warren C McNabb ◽  
Nicole C Roy ◽  
...  

Enzymatic hydrolysis of lactose is a crucial step to improve the efficiency and selectivity of membrane-based separations toward the recovery of milk oligosaccharides free from simple sugars. Response surface methodology was used to investigate the effects temperature (25.9 to 54.1 °C) and amount of enzyme (0.17 to 0.32% w/w) at 1, 2, and 4 h of reaction on the efficiency of lactose hydrolysis by Aspergillus oryzae β-galactosidase, preservation of major goat whey oligosaccharides, and on the de-novo formation of oligosaccharides. Lactose hydrolysis above 99% was achieved at 1, 2, and 4 h, not being significantly affected by temperature and amount of enzyme within the tested conditions. Formation of 4 Hexose (Hex) and 4 Hex 1 Hex and an increased de-novo formation of 2 Hex 1 N-Acetyl-Neuraminic Acid (NeuAc) and 2 Hex 1 N-Glycolylneuraminic acid (NeuGc) was observed in all treatments. Overall, processing conditions using temperatures ≤40 °C and enzyme concentration ≤0.25% resulted in higher preservation/formation of goat whey oligosaccharides.

2018 ◽  
Vol 17 (4) ◽  
pp. 349-354
Author(s):  
Qadir Rahman ◽  
Anwar Farooq ◽  
Amjad Gilani Mazhar ◽  
Nadeem Yaqoob Muhammad ◽  
Ahmad Mukhtar

This study investigates the effect of enzyme formulations (Zympex-014, Kemzyme dry-plus and Natuzyme) on recovery of phenolics from Peganum hermala (harmal) leaves, under optimized conditions using response surface methodology. As compared to the other enzyme complexes, the yield (34 g/100g) obtained through Zympex-014-assisted extraction was higher under optimized conditions such as time (75 min), temperature (70°C), pH (6.5) and enzyme concentration (5 g/100 g) using central composite design (CCD). Effectiveness of Zympex-014 towards hydrolysis of P. hermala leaves cell wall was examined by analyzing the control and enzyme-treated leave residues using scanning electron microscope (SEM). GC/MS characterization authenticated the presence of quercetin (1.44), gallic acid (0.23), caffeic acid (0.04), cinnamic acid (0.05), m-coumaric acid (0.23) and p-coumaric acid (0.37 μg/g) as the potent phenolics in Zympex-014 based extract. It can be concluded from the findings of the current work that pre-treatment of P. hermala leaves with Zympex-014 significantly enhanced the recovery of phenolics that supports its potential uses in the nutra-pharamaceutical industry.


2018 ◽  
pp. 19-20
Author(s):  
V.P. Panov ◽  
◽  
M.N. Koverda ◽  
B.G. Gavrilov ◽  
S.A. Kucherenkov ◽  
...  

2016 ◽  
Vol 19 (0) ◽  
Author(s):  
Ricardo Schmitz Ongaratto ◽  
Luiz Antonio Viotto

Summary The aim of this work was to separately evaluate the effects of pectinase and cellulase on the viscosity of pitanga juice, and determine the optimum conditions for their use employing response surface methodology. The independent variables were pectinase concentration (0-2.0 mg.g–1) and cellulase concentration (0-1.0 mg.g–1), activity time (10-110 min) and incubation temperature (23.2-56.8 °C). The use of pectinase and cellulase reduced the viscosity by about 15% and 25%, respectively. The results showed that enzyme concentration was the most important factor followed by activity time, and for the application of cellulase the incubation temperature had a significant effect too. The regression models showed correlation coefficients (R2) near to 0.90. The pectinase application conditions that led to the lowest viscosity were: concentration of 1.7 mg.g–1, incubation temperature of 37.6 °C and incubation time of 80 minutes, while for cellulase the values were: concentration of 1.0 mg.g-1, temperature range of 25 °C to 35 °C and incubation time of 110 minutes.


LWT ◽  
2013 ◽  
Vol 50 (1) ◽  
pp. 326-330 ◽  
Author(s):  
Gap-Don Kim ◽  
Tae-Chul Jung ◽  
Eun-Young Jung ◽  
Jin-Yeon Jeong ◽  
Han-Sul Yang ◽  
...  

2012 ◽  
Vol 84 (2) ◽  
pp. 443-454 ◽  
Author(s):  
Diego S. Nascimento ◽  
Gildomar Valasques Junior ◽  
Pedro Fernandes ◽  
Geise C.A. Ribeiro ◽  
Danyo M. Lima ◽  
...  

Inulinase (β-2,1-D- fructan fructanohydrolase), EC 3.2.1.7, targets the β-2,1 linkage of inulin, a polyfructan consisting of linear β-2,1 linked fructose, and hydrolyzes it into fructose. This use provides an alternative to produce fructose syrup through the hydrolysis of inulin. The objective of this work was to study the production, characterization and applications of inulinases from the fungal endophyte CCMB 328 isolated from the Brazilian semi-arid region. Response Surface Methodology (RSM) was employed to evaluate the effect of variables (concentration of glucose and yeast extract), on secreted inulinase activities detected in the culture medium and also in the inulin hydrolysis. The results showed that the best conditions for inulinase production by CCMB 328 are 9.89 g / L for glucose and 1.09 g / L for yeast extract. The concentration of 0.20 mol/L of NaCl and KCl increased the activity of inulinase from CCMB 328 by approximately 63% and 37%, respectively. The results also showed that the inulinase has potential for inulin hydrolysis, whose conversion yields roughly 72.48 % for an initial concentration of inulin at 1% (w/v).


1999 ◽  
Vol 30 (3) ◽  
pp. 265-271 ◽  
Author(s):  
Rubens Cruz ◽  
Vinícius D'Arcádia Cruz ◽  
Juliana Gisele Belote ◽  
Marcelo de Oliveira Khenayfes ◽  
Claudia Dorta ◽  
...  

<FONT FACE="Symbol">b</font>-Galactosidase or <FONT FACE="Symbol">b</font>-D-galactoside-galactohydrolase (EC. 3.2.1.23) is an important enzyme industrially used for the hydrolysis of lactose from milk and milk whey for several applications. Lately, the importance of this enzyme was enhanced by its galactosyltransferase activity, which is responsible for the synthesis of transgalactosylated oligosaccharides (TOS) that act as functional foods, with several beneficial effects on consumers. Penicillium simplicissimum, a strain isolated from soil, when grown in semi-solid medium showed good productivity of <FONT FACE="Symbol">b</font>-galactosidase with galactosyltransferase activity. The optimum pH for hydrolysis was in the 4.04.6 range and the optimum pH for galactosyltransferase activity was in the 6.07.0 range. The optimum temperature for hydrolysis and transferase activity was 55-60°C and 50°C, respectively, and the enzyme showed high thermostability for the hydrolytic activity. The enzyme showed a potential for several industrial applications such as removal of 67% of the lactose from milk and 84% of the lactose from milk whey when incubated at their original pH (4.5 and 6.34, respectively) under optimum temperature conditions. When incubated with a 40% lactose solution in 150 mM McIlvaine buffer, pH 4.5, at 55°C the enzyme converted 86.5% of the lactose to its component monosaccharides. When incubated with a 60% lactose solution in the same buffer but at pH 6.5 and 50°C, the enzyme can synthetize up to 30.5% TOS, with 39.5% lactose and 30% monosaccharides remaining in the preparation.


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