Lactose Assay Kit - Sequential/High Sensitivity

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00:04  Introduction
01:00  Principle
03:19   Reagent Preparation
04:23  Sample Preparation
05:37  Glucose Oxidase / Catalase Pre-Treatment
07:45  Procedure
11:08   Calculations

Lactose Assay Kit K-LOLAC Scheme
Reference code: K-LOLAC
SKU: 700004314

65 assays per kit

Content: 65 assays per kit
Shipping Temperature: Ambient
Storage Temperature: Short term stability: 2-8oC,
Long term stability: See individual component labels
Stability: > 2 years under recommended storage conditions
Analyte: Lactose
Assay Format: Spectrophotometer
Detection Method: Absorbance
Wavelength (nm): 340
Signal Response: Increase
Linear Range: 1 to 50 µg of lactose (or 0.50 to 25 µg of D-glucose)
Limit of Detection: 1.62 mg/L
Reaction Time (min): ~ 10 min
Method recognition: AOAC Method 2020.08

The K-LOLAC test kit offers a rapid, novel, sequential measurement of free-glucose and lactose in conventional, low-lactose and lactose-free dairy products. This sequential assay format reduces the manual input required by an analyst when compared to traditional lactose assay formats and therefore improves both accuracy and efficiency. When used in combination with the Megazyme Creep Calculator provided, the β-galactosidase employed in this kit allows for the selective measurement of lactose in the presence of galacto-oligosaccharides (GOS) which are commonly found in lactose-free dairy products. This constitutes a significant improvement over existing commercially available lactose assay kits which typically overestimate lactose content in lactose-free samples due to the unselective hydrolysis of GOS by β-galactosidase. Lastly, the sensitivity of the K-LOLAC assay kit has been doubled through the use of a cascade biochemical pathway, helping to significantly reduce the LOD and LOQ for the assay.

We offer more monosaccharide and oligosaccharide assay kit products.

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Scheme-K-LOLAC LOLAC Megazyme

Validation of Methods
  • World’s first sequential assay for lactose, i.e. improves accuracy and efficiency 
  • Contains a specific β-galactosidase for the selective measurement of lactose in dairy products 
  • Efficient pre-treatment step allows for accurate measurement of lactose in “low-lactose” and “lactose-free” dairy products 
  • Lower limit of detection (LOD) than any other commercially available enzymatic lactose detection method. LOD at 1.62 mg/L 
  • Very competitive price (cost per test)
Certificate of Analysis
Safety Data Sheet
FAQs Assay Protocol Data Calculator Validation Report
Megazyme publication

Lactose Concentration in Low-Lactose and Lactose-Free Milk, Milk Products, and Products Containing Dairy Ingredients by High Sensitivity Enzymatic Method (K-LOLAC), Collaborative Study: Final Action 2020.08.

Ivory, R., Mangan, D. & McCleary, B. V. (2022). Journal of AOAC International, qsac070.

Background: The AOAC Stakeholder Panel on Strategic Food Analytical Methods issued a call for methods in 2018 for the measurement of lactose in low-lactose and lactose-free products under Standard Method Performance Requirements (SMPR®) 2018.009. Megazyme's Lactose Assay Kit (K-LOLAC) was reviewed and accepted as a First Action Official Method in 2020 (2020.08). Objective: A collaborative study was conducted to evaluate the to evaluate the reproducibility of AOAC Method 2020.08 for the measurement of lactose concentration in low-lactose and lactose-free milk, milk products, and products containing dairy ingredients. Method: Samples are deproteinated and clarified by treatment with Carrez reagents, then free glucose is removed using a glucose oxidase and catalase treatment system. Quantification of lactose is based on the hydrolytic activity of β-galactosidase, which hydrolyses lactose to glucose and galactose. Any remaining free D-glucose is first measured using a Hexokinase (HK)/Glucose 6-phosphate dehydrogenase (G-6PDH)/6-phosphogluconate dehydrogenase (6-PGDH) based assay procedure, and then β-galactosidase is added to hydrolyse the lactose in the same reaction vessel with concurrent measurement of the released D-glucose. The samples analysed included a number of lactose free and low-lactose milk samples, lactose-free infant formula, lactose-free milkshake, lactose-free adult nutritional drink, lactose-free cream and lactose-free cheese. Results: All materials had repeatability relative standard deviations (RSDr) <7%. The reproducibility relative standard deviation (RSDR) varied from 3.8 to 14.9% with seven of the 10 test samples having an RSDR of < 10%. Conclusions: The Lactose Assay Kit (K-LOLAC) meets the requirements for reproducibility set out under SMPR 2018.009. Highlights: The Lactose Assay (K-LOLAC) is a robust, simple and reproducible method for analysis of lactose in foodstuffs and beverages.

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Megazyme publication

Determination of Lactose Concentration in Low-Lactose and Lactose-Free Milk, Milk Products, and Products Containing Dairy Ingredients: Single Laboratory Validation of an Enzymatic Method, First Action Method 2020.08.

Ivory, R., Delaney, E., Mangan, D. & McCleary, B. V. (2021).  Journal of AOAC International, qsab032.

Background: The AOAC Stakeholder Panel on Strategic Food Analytical Methods issued a call for methods for the measurement of lactose in low-lactose and lactose-free products under SMPR 2018.009 (1). Megazyme’s Lactose Assay Kit (K-LOLAC) was developed specifically to address the need for accurate enzymatic testing in lactose-free samples. Objective: The Lactose Assay (K-LOLAC) was validated for measurement of lactose in low-lactose and lactose-free milk, milk products, and products containing dairy ingredients. A single-laboratory validation of the method is reported. Method: The Lactose Assay (K-LOLAC) is an accurate and sensitive enzymatic method for the rapid measurement of lactose in low-lactose or lactose-free products. Validation analysis was performed on a sample set of 36 commercial food and beverage products and a set of 10 certified reference materials. Parameters examined during the validation included working range and linear range, selectivity, LOD, LOQ, trueness (bias), precision (repeatability and intermediate precision), robustness and stability. Results: For all samples tested within the lower range (10-100 mg/100 g or mL), recoveries varied from 93.21-14.10%. Recoveries obtained for samples in the higher range (>100 mg/100 g or mL) varied from 94.44-108.28%. All materials had repeatability relative standard deviations (RSDr and RSDir) of < 9%. Conclusions:  The commercial Lactose Assay Kit (K-LOLAC) as developed by Megazyme meets the requirements set out under SMPR 2018.009. Highlights: The Lactose Assay (K-LOLAC) is a robust, quick and easy method for analysis of lactose in foodstuffs and beverages.

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Megazyme publication

A novel enzymatic method for the measurement of lactose in lactose‐free products.

Mangan, D., McCleary, B. V., Culleton, H., Cornaggia, C., Ivory, R., McKie, V. A., Delaney, E. & Kargelis, T. (2018). Journal of the Science of Food and Agriculture, 99, 947-956.

Background: In recent years there has been a surge in the number of commercially available lactose‐free variants of a wide variety of products. This presents an analytical challenge for the measurement of the residual lactose content in the presence of high levels of mono‐, di‐, and oligosaccharides. Results: In the current work, we describe the development of a novel enzymatic low‐lactose determination method termed LOLAC (low lactose), which is based on an optimized glucose removal pre‐treatment step followed by a sequential enzymatic assay that measures residual glucose and lactose in a single cuvette. Sensitivity was improved over existing enzymatic lactose assays through the extension of the typical glucose detection biochemical pathway to amplify the signal response. Selectivity for lactose in the presence of structurally similar oligosaccharides was provided by using a β-galactosidase with much improved selectivity over the analytical industry standards from Aspergillus oryzae and Escherichia coli (EcLacZ), coupled with a ‘creep’ calculation adjustment to account for any overestimation. The resulting enzymatic method was fully characterized in terms of its linear range (2.3-113 mg per 100 g), limit of detection (LOD) (0.13 mg per 100 g), limit of quantification (LOQ) (0.44 mg per 100 g) and reproducibility (≤ 3.2% coefficient of variation (CV)). A range of commercially available lactose‐free samples were analyzed with spiking experiments and excellent recoveries were obtained. Lactose quantitation in lactose‐free infant formula, a particularly challenging matrix, was carried out using the LOLAC method and the results compared favorably with those obtained from a United Kingdom Accreditation Service (UKAS) accredited laboratory employing quantitative high performance anion exchange chromatography - pulsed amperometric detection (HPAEC‐PAD) analysis. Conclusion: The LOLAC assay is the first reported enzymatic method that accurately quantitates lactose in lactose‐free samples.

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Film-shaped reusable smart polymer to produce lactose-free milk by simple immersion.

Vallejo-García, J. L., Arnaiz, A., Busto, M. D., García, J. M. & Vallejos, S. (2023). European Polymer Journal, 200, 112495.

In this study, we report the synthesis and characterization of a highly manageable polyacrylic film material for enzyme immobilization, using β-galactosidase (β-gal) as a model enzyme. The material is based on commercially available monomers and achieves efficient immobilization of β-gal through the formation of azo linkages between amino styrene groups in the polyacrylic material and the enzyme. The immobilized enzyme demonstrates superior performance compared to free enzyme in lactose hydrolysis of UHT milk, achieving lactose concentrations below 0.1% (<1 mg/mL), indicating its potential for lactose hydrolysis in dairy products. The film-shaped material is designed for easy submersion and removal, similar to a smart card, and offers reusability, with the ability to be reused at least 10 times without loss of enzymatic activity. Characterization of the immobilized enzyme on the polymeric material was performed using various techniques, including scanning electron microscopy (SEM), Fourier-transform infrared spectroscopy (FT-IR), and Raman spectroscopy. Protein release studies confirmed the stability of the immobilized enzyme during prolonged incubation in aqueous solution without significant enzyme leakage. Overall, the polyacrylic film material demonstrates promise as a simple and efficient approach for enzyme immobilization, with potential applications in various industries, including the food industry.

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Effects of lactose hydrolysis and milk type on the quality of lactose-free yoghurt.

Popescu, L., Bulgaru, V. & Siminiuc, R. (2022). Journal of Engineering Sciences, (4), 164-175.

The purpose of the work was to investigate the influence of different lactose hydrolysis processes, the contribution of the enzyme and the milk type on the characteristics of the obtained lactose-free yogurt. The analysis was performed on non-hydrolyzed yogurt (control sample), the pre-hydrolyzed yogurt (that was hydrolyzed before fermentation), and the co-hydrolyzed yogurt (concurrent addition of β-galactosidase and starter culture). According to the obtained results, at the end of the fermentation time, an advanced hydrolysis degree was reached (over 80%) both for yogurt samples obtained from pre-hydrolyzed milk and obtained by co-hydrolysis. The optimal method from the economic point of view is to obtain yogurt by co-hydrolysis. The sensory quality of the yogurt samples obtained from hydrolyzed milk by co-hydrolysis was characterized by a better flavor than the control sample, for yogurt from both types of milk. This may be due to the availability of a greater amount of glucose for the production of aromatic compounds, a sweeter taste than natural yogurt, with a light caramel flavor, a firm coagulum, a porcelain appearance, without whey removal. Cow's milk yogurt showed higher viscosity values to goat's milk yogurt for both pre-hydrolyzed and co-hydrolyzed milk. Lactose hydrolysis determined the reduction of the syneresis index of the yogurt compared to the control samples. The studies led to the development of lactose-free yogurt with improved sensory and rheological properties recommended for people with lactose intolerance.

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Blood neutrophil extracellular traps: a novel target for the assessment of mammary health in transition dairy cows.

Jiang, L., Sun, H., Gu, F., He, J., Zhao, F. & Liu, J. (2022). Journal of Animal Science and Biotechnology, 13(1), 1-12.

Background: Mammary health is important for transition dairy cows and has been well recognized to exert decisive effects on animal welfare. However, the factors influencing mammary health are still unclear. Differential somatic cell count (DSCC) could reflect the mastitis risk since it is the percentage of neutrophils plus lymphocytes in total somatic cells and could be reflective of mammary health of dairy cows. This work aimed to investigate the assessment and prognosis of the health of transition cows based on blood neutrophil extracellular traps (NETs). Results: Eighty-four transition Holstein dairy cows were selected. The serum was sampled in all the animals at week 1 pre- and postpartum, and milk was sampled at week 1 postpartum. Based on the DSCC in milk at week 1, cows with lower (7.4% ± 4.07%, n = 15) and higher (83.3% ± 1.21%, n = 15) DSCCs were selected. High DSCC cows had higher levels of red blood cell counts (P < 0.05), hemoglobin (P = 0.07), and hematocrit (P = 0.05), higher concentrations of serum oxidative variables [(reactive oxygen species (P < 0.05), malondialdehyde (P < 0.05), protein carbonyl (P < 0.05), and 8-hydroxy-2-deoxyguanosine (P = 0.07)], higher levels of serum and milk NETs (P < 0.05) and blood-milk barrier indicators, including serum β-casein (P = 0.05) and milk immunoglobulin G2 (P = 0.09), than those of low DSCC cows. In addition, lower concentrations of serum nutrient metabolites (cholesterol and albumin) (P < 0.05) and a lower level of serum deoxyribonuclease I (P = 0.09) were observed in high DSCC cows than in low DSCC cows. Among the assessments performed using levels of the three prepartum serum parameters (NETs, deoxyribonuclease I and β-casein), the area under the curve (0.973) of NETs was the highest. In addition, the sensitivity (1.00) and specificity (0.93) were observed for the discrimination of these cows using NETs levels with a critical value of 32.2 ng/mL (P < 0.05). Conclusions: The formation of NETs in blood in transition dairy cows may damage the integrity of the blood-milk barrier and thereby increase the risk for mastitis in postpartum cows.

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

Popescu, L., Bulgaru, V. & Siminiuc, R. (2021). Food and Nutrition Sciences, 12(12), 1243-1254.

Lactose intolerance is becoming a health state that requires the restriction of dairy products in the diet of people suffering from this condition. But milk and dairy products, due to a well-balanced composition in the main macro and micronutrients, cannot be missing from the diet of the consumer of any age. For these reasons, in recent years, in the milk processing industry, the production of low-lactose or lactose-free dairy products is explored. To reduce the lactose content of dairy raw materials, various industrial and biotechnological methods were used: enzymatic hydrolysis of lactose, baromembranous methods, bioconversion of lactose by lactic bacteria and others. The most widely used lactase enzymes in the industry are mesophilic enzymes from filamentous fungi (Aspergillus spp.) and yeasts (Kluyveromyces spp.). Therefore, the aim of this study was to evaluate the effect of the commercial enzyme β-galactosidase on the hydrolysis of cow’s milk at different enzyme concentrations, temperatures and pH. Two commercial enzymes β-galactosidase obtained from Bacillus licheniformis and β-galactosidase obtained from Kluyveromyces lactis, were used in this study, according to information provided by the manufacturer. The thermal stability of lactose, the effect of milk pH, the effect of temperature, duration of hydrolysis and the amount of enzymes on the lactose hydrolysis degree and the sweetness degree of milk were determined. Research has identified the optimal parameters for obtaining a high degree of lactose hydrolysis in the use of these enzymes. Therefore, to ensure a high lactose hydrolysis degree (over 80%), the following lactose hydrolysis regimens were identified: temperature 4°C - 6°C, 0.3% Bacillus licheniformis enzymes, duration 4 hours; temperature 4°C - 6°C, 0.3% enzymes from Klavyromyces lactis, duration 12 hours and temperature 38°C - 40°C, 0.15% enzymes from (Bacillus licheniformis or Klavyromyces lactis), duration 2 - 3 hours. The results obtained allow the efficient use of Bacillus licheniformis and Klavyromyces lactis enzymes in industrial processes for the manufacture of “lactose-free” or “low-lactose” drinking milk and fermented dairy products for people with lactose intolerance.

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Fermentation Ability of Bovine Colostrum by Different Probiotic Strains.

Hyrslova, I., Krausova, G., Michlova, T., Kana, A. & Curda, L. (2020). Fermentation, 6(3), 93.

Over the past decade, the use of bovine colostrum and its bioactive components as the basis of functional food and dietary supplements for humans has substantially increased. However, for developing new products enriched with probiotics and bovine colostrum, the influence of colostrum composition on the growth promotion of bacteria still needs to be tested. Therefore, we decided to study the influence of bovine colostrum chemical and mineral composition as well as the content of bioactive compounds (immunoglobulins, lactoferrin, lactoperoxidase) on the growth of ten selected strains from genera Lactobacillus, Lacticaseibacillus, Bifidobacterium, and Enterococcus. After 24 h of fermentation, the growth was assessed based on lactic and acetic acids production evaluated using isotachophoresis, bacterial counts determined by the agar plate method, and change of pH. The production of acids and bacterial counts were significantly (P<0.05) different between selected genera. The change of bacterial counts was correlated with pH, but the correlation between growth and bovine colostrum composition was not proven. The highest growth and production of lactic acid was observed after the fermentation of bovine colostrum by the strains Enterococcus faecium CCDM 922A and CCDM 945.

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Exploring the potential of microalgae in the recycling of dairy wastes.

Gramegna, G., Scortica, A., Scafati, V., Ferella, F., Gurrieri, L., Giovannoni, M., Bassi, R., Sparla, F., Mattei, B. & Benedetti, M. (2020). Bioresource Technology Reports, 12, 100604.

Culturing microalgae using dairy-wastes offers the opportunity of producing valuable biomass for different industrial applications. The capability of four Chlorella species and a recombinant Chlamydomonas reinhardtii strain to mixotrophically grow in wastewaters from an Italian dairy factory was investigated. A robust algal growth could be efficiently sustained in these wastes, despite the abundance of D-Lactose (~4% w/v), that could not be metabolized by any microalgal species. Non axenic cocultivation of microalgae together with microbial communities from the dairy wastes resulted in a marked decrease of their pollution load, thus reducing the necessity of expensive treatments before their discharge in the municipal sewage system. Microalgae cultivated using dairy-wastes were characterized by a lipid content ranging from 12% to 21% (w/w), with Auxenochlorella protothecoides reaching the highest lipid productivity (~0.16 g/L/d) whereas the transplastomic C. reinhardtii strain expressing a thermostable β-glucosidase reached a recombinant enzyme productivity of 0.18 mg/L/d.

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GRP78 regulates milk biosynthesis and the proliferation of bovinemammaryepithelial cells through the mTOR signaling pathway.

Liu, Y., Wang, X., Zhen, Z., Yu, Y., Qiu, Y. & Xiang, W. (2019). Cellular & molecular biology letters, 24(1), 1-12.

Methods: The expressions of GRP78 in BMECs stimulated with methionine, leucine, estrogen and prolactin were determined using western blotting and immunofluorescence assays. To explore the function of GRP78 in BMECs, the protein was overexpressed or knocked down, respectively using an overexpression vector or an siRNA mixture transfected into cells cultured in vitro. Flow cytometry was used to analyze cell proliferation and cell activity. The contents of lactose and triglyceride (TG) secreted from the treated BMECs were measured using lactose and TG assay kits, respectively. Western blotting analysis was used to measure the β-casein content and the protein levels of the signaling molecules known to be involved in milk biosynthesis and cell proliferation. Results: GRP78overexpression significantly stimulated milk protein and milk fat synthesis, enhanced cell proliferation, positively regulated the phosphorylation of mammalian target of rapamycin (mTOR), and increased the amount of protein of cyclinD1andsterol regulatory element-binding protein 1c (SREBP-1c). GRP78 knockdown after siRNA transfection had the opposite effects. We further found that GRP78 was located in the cytoplasm of BMECs, and that stimulating methionine, leucine, estrogen and prolactin expression led to a significant increase in the protein expression of GRP78 in BMECs. Conclusions: These data reveal that GRP78 is an important regulator of milk biosynthesis and the proliferation of BMECs through the mTOR signaling pathway.

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Comparative study of two lactases by K-Lolac enzymatic method in skimmed milk. 

Benbouziane, B., Bentahar, M. C., Takarly, H. & Benakriche, B. M. (2019). South Asian Journal of Experimental Biology, 9(1), 1-6.

Lactose absorption at the level of the small intestine depends on its hydrolysis by β-galactosidase. The activity of this enzyme, which gets to the peak at the beginning and halflife, decreases progressively after weaning. This activity loss (hypolactasie) is a physiological phenomenon observed in 70 to 75% of the world's population. Hypolactasy is transmitted according to an autosomal recessive mode to an incomplete penetrance and is linked to polymorphosis located in the promoter region of the gene coding the lactase. A solution is proposed regarding ingestion of dairy dislactosed products or products with unduly low lactose rates. In this study, two different enzymes were used, a β-galactosidase of Bifidobacterium [β-gal Bb] source and another β-galactosidase of Kluyveromyces lactis [β-gal Kl] source with different concentrations on lactose degradation in a preparation based on skimmed milk at 4°C during 18h with a 39 g/l lactose rate. Determining hydrolysis rate in lactose was achieved with an enzymatic method using a Megazyme K-lolac kit. The results demonstrated that β-gal Kl (Maxilat) in a 100 µl/L dose gives an optimal performance as compared to β-gal Bb (Nola fit) in residual lactose concentrations 1.85 g/L and 2.78 g/L respectively. However, in a dose that was superior to 1500 and 2000, the β-gal Bb was significantly more performing than β-gal Kl. To sum up, the enzymatic method used to define the residual lactose rate, the kit KLolac, gives very reliable results with a low threshold (LOD 1.62 mg/L).

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Lactose-free Yogurts do not Show any Benefits for Lactose-Intolerant Subjects, Compared with Lactose-Containing Yogurts. 

Ghio, B., Márquez, D., Peche, B., Peña, F. & Saavedra, F. (2019). Journal of Food & Nutritional Disorders, 8(3), 2.

Nowadays, there is constant increase of commercial lactose-free yogurts for lactose-intolerant individuals. However, the real interest of these yogurts is unclear considering that several clinical trials have shown that the living bacteria present in the yogurt improved lactose tolerance in hypolactasic subjects, due to their β-galactosidase activity that remains functional in the small intestine of these individuals. The aim of this study was to determine whether the intake of lactose-free yogurt (LFY) is beneficial for hypolactasic lactose-intolerant subjects compared with that of traditional, lactose-containing yogurt (LCY). Twenty-two subjects with auto-reported digestive symptoms after milk consumption carried out a hydrogen breath test (HBT) with 25g lactose to confirm their hypolactasic status. Fourteen subjects (63.6%) who exhibit a positive HBT accompanied by digestive symptoms were finally incorporated to the study. In two independent days, they have to ingest, in a double-blind and randomized form, 250g of LFY or LCY. These products brought 0.5g and 19.8g of lactose, respectively and both exhibited total counts of lactic acid bacteria higher than 107 CFU/g. Changes in breath H2 excretion and digestive symptoms were registered during 180 min. When the volunteers carried out the HBT with LFY and LCY, no differences were detected in H2 excretion or the intensity of digestive symptoms (individual or total). Accordingly, our results suggest than the intake of LFY that are more expensive than LCY, does not bring any supplementary detectable benefits for the lactose intolerant subjects.

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Influence of particle size on the physicochemical properties and stickiness of dairy powders.

O'Donoghue, L. T., Haque, M. K., Kennedy, D., Laffir, F. R., Hogan, S. A., O'Mahony, J. A. & Murphy, E. G. (2019). International Dairy Journal, 98, 54-63.

The compositional and physicochemical properties of different whey permeate (WPP), demineralised whey (DWP) and skim milk powder (SMP) size fractions were investigated. Bulk composition of WPP and DWP was significantly (P < 0.05) influenced by powder particle size; smaller particles had higher protein and lower lactose contents. Microscopic observations showed that WPP and DWP contained both larger lactose crystals and smaller amorphous particles. Bulk composition of SMP did not vary with particle size. Surface composition of the smallest SMP fraction (<75 µm) showed significantly lower protein (−9%) and higher fat (+5%) coverage compared with non-fractionated powders. For all powders, smaller particles were more susceptible to sticking. Hygroscopicity of SMP was not affected by particle size; hygroscopicity of semi-crystalline powders was inversely related to particle size. This study provides insights into differences between size fractions of dairy powders, which can potentially impact the sticking/caking behaviour of fine particles during processing.

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Accurate analysis of residual lactose in low-lactose milk: Comparing a variety of analytical techniques.

Churakova, E., Peri, K., Vis, J. S., Smith, D. W., Beam, J. M., Vijverberg, M. P., Stor, M. C. & Winter, R. T. (2019). International Dairy Journal, 96, 126-131.

To receive the designation “lactose-free”, milk should contain <0.01% (w/w) lactose. As the analysis of such low levels of lactose is often hampered by other saccharides present or formed during milk processing, methods are required that are highly sensitive, accurate and precise. Currently, there is no international standard analysis method for the determination of lactose in low- or lactose-free milk, despite such a need from the dairy industry. We validated the analysis of residual lactose in lactase-treated UHT milk using HPAEC-PAD on a CarboPac PA100 column and compared it with a variety of commonly used analytical techniques for measuring lactose, including HPLC-RI, NMR, enzymatic kits, cryoscopy, and lactose biosensors. The results show that only one analytical technique, namely the Biomilk300, an amperometric biosensor, has performance comparable with analysis by HPAEC-PAD, which remains one of the most accurate, precise and sensitive methods to assess low levels of lactose in milk.

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Safety Information
Symbol : GHS05, GHS07, GHS08
Signal Word : Danger
Hazard Statements : H302, H302+H332, H314, H334, H360
Precautionary Statements : P201, P202, P260, P261, P264, P270, P271, P280, P284, P301+P312, P301+P330+P331, P304+P340, P342+P311, P501
Safety Data Sheet
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