scholarly journals Effect of Temperature, pH and Amount of Enzyme Used in the Lactose Hydrolysis of Milk

2021 ◽  
Vol 12 (12) ◽  
pp. 1243-1254
Author(s):  
Liliana Popescu ◽  
Viorica Bulgaru ◽  
Rodica Siminiuc
1986 ◽  
pp. 221-221
Author(s):  
J. F. Hayes ◽  
I. Mitchell ◽  
M. Free ◽  
J. G. Zadov

1989 ◽  
Vol 257 (4) ◽  
pp. G616-G623 ◽  
Author(s):  
H. A. Buller ◽  
A. G. Van Wassenaer ◽  
S. Raghavan ◽  
R. K. Montgomery ◽  
M. A. Sybicki ◽  
...  

Lactase-phlorizin hydrolase, a small intestinal disaccharidase, has been considered mainly an enzyme important only for the hydrolysis of lactose. After weaning in most mammals lactase-specific activity falls markedly, and, functionally, adult mammals are considered to be lactase deficient. However, the persistence of low levels of lactase activity in adulthood has never been explained. In addition, it has been suggested that lactase-phlorizin hydrolase is associated with glycosylceramidase activity when the enzyme is prepared by column chromatography, but it is unclear whether this represents copurified activities or two catalytic sites on one peptide. The developmental patterns of lactase-phlorizin hydrolase and other disaccharidases were investigated in homogenates of total rat small intestine; lactase and several glycosylceramidases were measured in immunoprecipitates from these homogenates using a monoclonal antibody. The developmental pattern of total lactase activity showed a steady 2.3-fold increase to adult levels (specific activity decreased eightfold), whereas total phlorizin-hydrolase activity increased 10.7-fold (specific activity decreased threefold). As expected, levels of both total and specific sucrase and maltase activities increased during development. In lactating rats total lactase activity showed a significant increase compared with adult males. The developmental pattern of the enzyme activities for the glycolipid substrates was similar to that found for lactase, and the immunoprecipitated enzyme showed a 40- to 55-fold higher affinity for the glycolipids than for lactose. Galactosyl- and lactosylceramide inhibited lactose hydrolysis by 38%, without a competitive pattern, suggesting two different active sites for lactose and glycolipid hydrolysis, respectively.(ABSTRACT TRUNCATED AT 250 WORDS)


2018 ◽  
Vol 152 ◽  
pp. 01014 ◽  
Author(s):  
Yoon Li Wan ◽  
Yuen Jun Mun

Before the conversion of lignocellulosic biomass into fuel such as ethanol, the biomass needs to be pretreated and the yield of ethanol is highly dependent on the pretreatment efficiency. This study investigate the performance of deep eutectic solvent (DES) in pretreating sago waste which is a type of starchy biomass. The suitable type of DES in sago waste pretreatment was selected based on three criteria, which is the structural characteristic, the sugar yield during enzymatic hydrolysis and the amount of sugar loss during pretreatment. In this study, three types of DES namely Choline Chloride-Urea (ChCl-Urea), Choline Chloride-Citric acid (ChCl-CA) and Choline Chloride-Glycerol (ChCl-Glycerol) was investigated. The effect of temperature and duration on DES pretreatment was also investigated. All DES reagents were able to disrupt the structure and increase the porosity of sago waste during pretreatment. ChCl-Urea was selected in this study as it shows apparent structural disruption as examined under Scanning Electron Microscope (SEM). The highest glucose yield of 5.2 mg/mL was derived from enzymatic hydrolysis of ChCl-Urea pretreated sago waste. Moreover, reducing sugar loss during ChCl-Urea pretreatment was low, with only 0.8 mg/mL recorded. The most suitable temperature and duration for ChCl-Urea pretreatment is at 110°C and 3 hr. In a nutshell, the application of DES in pretreatment is feasible and other aspects such as the biodegradability and recyclability of DES is worth investigating to improve the economic feasibility of this pretreatment technique.


2014 ◽  
Vol 77 (12) ◽  
pp. 2133-2138 ◽  
Author(s):  
AMIN N. OLAIMAT ◽  
BABAK SOBHI ◽  
RICHARD A. HOLLEY

Factors, including pH, temperature, glucose concentration, and iron compounds, affect the activity of plant myrosinase and, consequently, endogenous glucosinolate degradation. These factors also may affect glucosinolate degradation by bacterial myrosinase. Therefore, this study examined the effect of temperature (4 to 21°C), glucose (0.05 to 1.0%), and iron (10 mM ferrous or ferric) on sinigrin degradation by Salmonella or Listeria monocytogenes cocktails in Mueller-Hinton broth and the effect of sinigrin degradation on bacterial viability. The degradation of sinigrin by both pathogens increased with higher temperatures (21 > 10 > 4°C). Salmonella and L. monocytogenes cocktails hydrolyzed 59.1 and 53.2% of sinigrin, respectively, at 21°C up to 21 days. Both iron compounds significantly enhanced sinigrin degradation by the pathogens. On day 7, sinigrin was not detected when the Salmonella cocktail was cultured with ferrous iron or when the L. monocytogenes cocktail was cultured in Mueller-Hinton broth containing ferric iron. In contrast, ferric and ferrous iron inhibited the activity of 0.002 U/ml myrosinase from white mustard by 63 and 35%, respectively, on day 1. Salmonella and L. monocytogenes cocktails were able to degrade >80% of sinigrin at 0.05 and 0.1% glucose; however, 0.25 to 1.0% glucose significantly reduced sinigrin degradation. Although both pathogens significantly degraded sinigrin, the allyl isothiocyanate (AITC) recoverable was ≤6.2 ppm, which is not inhibitory to Salmonella or L. monocytogenes. It is probable that the gradual hydrolysis of sinigrin to form AITC either did not produce an inhibitory level of AITC or the AITC formed was unstable in the aqueous medium and rapidly decomposed to new compounds that were less bactericidal against the pathogens.


Author(s):  
Massimo Poletto ◽  
Palma Parascandola ◽  
Ivan Saracino ◽  
Giuseppe Cifarelli

The purpose of this work is to verify the possibility of using a simple physical adsorption technique to improve enzyme efficiency in performing lactose hydrolysis. Immobilization experiments of ß -galactosidase on zeolite pellets showed that this process is fairly slow and can be accomplished with contact times shorter than few hours. Comparison between homogeneous and heterogeneous hydrolysis experiments in mixed batch reactors indicates that the enzyme distribution within the zeolite pellets is concentrated in a thin shell under the pellet surface. Continuous conversion experiments were carried out on a purposely-built fluidization column. Results were fitted with a mathematical model for fluidized bed conversion without the use of any further adjustable parameter than those used in the heterogeneous batch conversion. Furthermore, no change of the parameter values was necessary. Scale-up predictions given by the model showed that fluidized columns few meters high of pellets supporting b-galactosidase are sufficient for an industrially suitable process of lactose hydrolysis. which can be performed on columns of few meters and, therefore, these are applicable to relatively small process scales as those found in traditional Italian cheese making factories.


2021 ◽  
Author(s):  
Zhi-Peng Wang ◽  
Jing-Run Ye ◽  
Yan Ma ◽  
Xin-Yue Zhang ◽  
Hai-ying Wang ◽  
...  

Abstract BackgroundRaw materials composed of easily assimilated monosaccharides have been employed as carbon source for production of microbial lipids. Nevertheless, agro-industrial wastes rich in galactose-based carbohydrates have not been introduced as feedstocks for oleaginous yeasts. ResultsIn this study, Aureobasidium namibiae A12 was found to efficiently accumulate lipid from soy molasses and whey powder containing galactose-based carbohydrates, with lipid productions of 5.30 g/L and 5.23 g/L, respectively. Over 80% of the fatty acids was C16:0, C18:0, C18:1, and C18:2. All kinds of single sugar components in the two byproducts were readily converted into lipids, with yields ranging between 0.116 g/g and 0.138 g/g. Three α-galactosidases and five β-galactosidases in the strain were cloned and analyzed. β-galactosidase was responsible for lactose hydrolysis; sucrase and α-galactosidase both contributed to the efficient hydrolysis of raffinose and stachyose in a cooperation manner. ConclusionsThis is a new way to produce lipids from raw materials containing galactose-based carbohydrates. This finding revealed the significance of sucrase in the direct hydrolysis of galactose-based carbohydrates in raw materials for the first time and facilitated the understanding of the efficient utilization of galactose-based carbohydrates to manufacture lipid or other chemicals in bioprocess


Marine Drugs ◽  
2020 ◽  
Vol 18 (6) ◽  
pp. 312 ◽  
Author(s):  
Dandan Li ◽  
Shangyong Li ◽  
Yanhong Wu ◽  
Mengfei Jin ◽  
Yu Zhou ◽  
...  

As prebiotics, galacto-oligosaccharides (GOSs) can improve the intestinal flora and have important applications in medicine. β-galactosidases could promote the synthesis of GOSs in lactose and catalyze the hydrolysis of lactose. In this study, a new β-galactosidase gene (gal2A), which belongs to the glycoside hydrolase family 2, was cloned from marine bacterium Alteromonas sp. QD01 and expressed in Escherichia coli. The molecular weight of Gal2A was 117.07 kDa. The optimal pH and temperature of Gal2A were 8.0 and 40 °C, respectively. At the same time, Gal2A showed wide pH stability in the pH range of 6.0–9.5, which is suitable for lactose hydrolysis in milk. Most metal ions promoted the activity of Gal2A, especially Mn2+ and Mg2+. Importantly, Gal2A exhibited high transglycosylation activity, which can catalyze the formation of GOS from milk and lactose. These characteristics indicated that Gal2A may be ideal for producing GOSs and lactose-reducing dairy products.


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