Behaviour ofYersinia enterocolitica andAeromonas hydrophila in skim milk during fermentation by various lactobacilli

In this study, behaviour ofYersinia enterocolitica andAeromonas hydrophila in skim milk during fermentation by various_{lactobacillus} sp. were determined. pH values of the skim milk samples were also examined during fermentation. The amount of produced lactic acid and diacetyl/acetoin productions of theLactobacillus sp. were estimated. Antimicrobial effects of the lactobacilli onY. enterocolitica andA. hydrophila were also determined by an agar diffusion method. WhileY. enterocolitica was not inhibited and grew during fermentation,A. hydrophila was inhibited, in part, and the growth was retarded. Results were supported by the agar diffusion method forY. enterocolitica, whereas inhibition activity was not found forA. hydrophila. The highest lactic acid productions were estimated inL. bulgaricus (7.50 mg/ml) andL. acidophilus (5.63 mg/ml) and four out of sixLactobacillus sp. were found to be diacetyl/acetoin producers.     

Behaviour ofYersinia enterocolitica andAeromonas hydrophila in skim milk during fermentation by various lactobacilli

In this study, behaviour ofYersinia enterocolitica andAeromonas hydrophila in skim milk during fermentation by various_{lactobacillus} sp. were determined. pH values of the skim milk samples were also examined during fermentation. The amount of produced lactic acid and diacetyl/acetoin productions of theLactobacillus sp. were estimated. Antimicrobial effects of the lactobacilli onY. enterocolitica andA. hydrophila were also determined by an agar diffusion method. WhileY. enterocolitica was not inhibited and grew during fermentation,A. hydrophila was inhibited, in part, and the growth was retarded. Results were supported by the agar diffusion method forY. enterocolitica, whereas inhibition activity was not found forA. hydrophila. The highest lactic acid productions were estimated inL. bulgaricus (7.50 mg/ml) andL. acidophilus (5.63 mg/ml) and four out of sixLactobacillus sp. were found to be diacetyl/acetoin producers.     

Partitioning of nitroxynil,oxyclozanide and levamisole residues from milk to cream,skim milk and skim milk powder

Veterinary drugs are necessary to control fluke in animals, and if not properly used, residues of these drugs may be found in milk. The aim of this study was to determine whether residues of nitroxynil, levamisole and oxyclozanide in milk partition into skim milk powder during processing. Milk targeted to contain high, medium or low levels of residue was obtained following treatment of trial animals. On separation of cream and skim milk, > 90% of the residue partitioned with the skim milk in all cases. During powder processing, the residues were not degraded with almost 90% of the residue detected in the powder.     

Formation of oligosaccharides in skim milk fermented with mixed dahi cultures, Lactococcus lactis ssp diacetylactis and probiotic strains of lactobacilli

Milk fermented with mixed dahi cultures NCDC167, Lactococcus lactis ssp diacetylactis NCDC60 and two probiotic strains; Lactobacillus acidophilus NCDC14 and Lb. casei NCDC19 were evaluated after fermentation (14 h) and during 8 d storage at 7 degrees C. The beta-galactosidase activity was found to increase after fermentation leading to the hydrolysis of lactose and production of glucose, galactose and oligosaccharides; that subsequently decreased during storage. The viable counts of lactococci and lactobacilli decreased during storage yet remained >106 cfu/ml after storage. The results of present study indicate that all the selected cultures have ability to produce oligosaccharides (prebiotics) due to transgalactosidal and lactose hydrolysis activities of beta-galactosidase. The cultures developed an active synbiotic formula by maintaining sufficient probiotic viable counts to exert health benefits to the consumers.     

Physico-chemical characterization of phosphate-added skim milk

The addition of potassium phosphate (KH₂PO₄) to milk is a common practice in the dairy industry but the changes resulting from such addition have not been fully elucidated. Physico-chemical changes were evaluated after addition of KH₂PO₄ at concentrations from 0 to 160 mm with or without adjustment of pH. At pH adjusted to 6.8, the addition of phosphate to milk-induced formation of insoluble calcium phosphate salt, decrease in lightness and solubilization of casein molecules. As a result of these biochemical changes, especially at high phosphate concentrations (about 120 mm and more), the formation of large aggregates occurred. At the same time, the amount of water combined with the modified casein strongly increased. When the pH was not adjusted, the same biochemical changes occurred but they were quantitatively lower. In this case, no destabilization of casein micelles occurred.     

低热脱脂奶粉的生产现状

综述了我国脱脂奶粉的的市场和生产现状,提出了向低热脱脂奶粉发展的方向,论述了加工条件对脱脂奶粉蛋白变性程度的影响以及国际上对奶粉热分级的规定和乳粉加工中乳清蛋白热变性及聚合物产生机理的研究进展。     

Acidification of lactoferrin-casein micelle complexes in skim milk

Lactoferrin electrostatically bound to the casein micelles when added to milk, which caused the absolute zeta potential to decrease and the micelle size to increase. On acidification, the lactoferrin progressively dissociated from the micelles, which, at pH below ∼5.0, caused the zeta potential of the casein micelles to be the same as those in milk without added lactoferrin. Acidification caused increased levels of casein to dissociate from the casein micelles at ∼pH 5.0 as the level of added lactoferrin in the milk increased. Lactoferrin decreased the pH at which the milk gelled and caused the G′ and yield stress of the set gels to increase at low levels of added lactoferrin, decrease at intermediate levels of added lactoferrin and increase again at high levels of added lactoferrin. This unusual effect of lactoferrin on gelation was hypothesised to be due to combined effects of dissociated casein and the lower gelation pH.     

Detection and inactivation of saxitoxin in skim milk

In this study, saxitoxin dihydrochloride in skim milk was reacted with sodium hydroxide and hydrogen peroxide to yield nontoxic 8-amino-6-hydroxymethyl-iminopurine-3(2H)-propionic acid (AHIPA), which was quantified by fluorescence spectroscopy using excitation and emission wavelengths of 330 and 425 nm, respectively. Samples of saxitoxin dihydrochloride (in 20% ethanol, vol/vol) were used as controls. The limits of detection of AHIPA, based on the concentration of saxitoxin prior to inactivation, were 5 and 10 μg/ml for the control and skim milk, respectively. These values are considerably below the concentration of saxitoxin that corresponds to the lethal dosage of 1 mg for an adult of average weight (70 kg). The inactivation of saxitoxin proceeded at a lower rate in skim milk than in the control, as its reaction rate constant was only 0.004 min(-1) compared with 0.011 min(-1) for the control. We were unable to detect AHIPA in 2% milk contaminated with saxitoxin because of possible interference from what we believed were products of secondary reactions involving milk fat and sodium hydroxide. Our results also indicated that the conversion of saxitoxin to AHIPA increased initially with temperature up to 40°C but decreased thereafter. We observed a decrease in the formation of AHIPA when the concentration of hydrogen peroxide was increased except at 22°C, where there was an initial increase in AHIPA formation between 1.2 and 2.4 mg/ml hydrogen peroxide but its formation decreased thereafter.     

State of unesterified fatty acids in skim milk

By a multiple extraction procedure the unesterified fatty acids of skim milk have been shown in at least three entities: a) free dissociated and undissociated fatty acids, b) fatty acids associated with the membrane material in skim milk, and c) fatty acids of unknown origin requiring acidification to pH 1.5 for extraction.     

Dairy cow feeding system alters the characteristics of low-heat skim milk powder and processability of reconstituted skim milk

Low-heat skim milk powder (LHSMP) was manufactured on 3 separate occasions in mid lactation (ML, July 4–20) and late lactation (LL, September 27 to October 7) from bulk milk of 3 spring-calving dairy herds on different feeding systems: grazing on perennial ryegrass (Lolium perenne L.) pasture (GRO), grazing on perennial ryegrass and white clover (Trifolium repens L.) pasture (GRC), and housed indoors and offered total mixed ration (TMR). The resultant powders (GRO-SMP, GRC-SMP, and TMR-SMP) were evaluated for composition and color and for the compositional, physicochemical, and processing characteristics of the reconstituted skim milk (RSM) prepared by dispersing the powders to 10% (wt/wt) in water. Feeding system significantly affected the contents of protein and lactose, the elemental composition, and the color of the LHSMP, as well as the rennet gelation properties of the RSM. The GRO and GRC powders had a higher protein content; lower levels of lactose, iodine, and selenium; and a more yellow-green color (lower a* and higher b* color coordinates) than TMR powder. On reconstitution, the GRO-RSM had higher concentrations of protein, casein, and ionic calcium, and lower concentrations of lactose and nonprotein nitrogen (% of total N). It also produced rennet gels with a higher storage modulus (G′) than the corresponding TMR-RSM. These effects were observed over the combined ML and LL period but varied somewhat during the separate ML and LL periods. Otherwise, feeding system had little or no effect on proportions of individual caseins, concentration of serum casein, casein micelle size, casein hydration, heat coagulation time, or ethanol stability of the RSM at pH 6.2 to 7.2, or on the water-holding capacity, viscosity, and flow behavior of stirred yogurt prepared by starter-induced acidification of RSM. The differences in the functionality of the LHSMP may be of greater or lesser importance depending on the application and the conditions applied during the processing of the RSM.     

Age gelation in UHT-processed reconstituted concentrated skim milk

UHT reconstituted concentrated skim milks made from high-heat powder had considerably longer gelation times than those made from medium- or low-heat powders. Addition of hexametaphosphate to the concentrated milk before UHT processing markedly delayed the onset of gelation during storage. Sediment formation was greatest in the UHT concentrated skim milk made using high-heat powder followed by samples made using medium- and low-heat powders, respectively. The extent of proteolysis, as measured by 12% TCA-soluble amino groups, increased at a faster rate in the UHT milks stored at 40°C than in those stored at 22°C but decreased with increasing heat treatment of the milk prior to powder manufacture. The electrophoretic patterns of samples stored at 22°C clearly showed the breakdown of β-casein with a corresponding increase in slower moving bands, presumably γ-casein and proteose-peptone components. However, storage of samples at 40°C resulted in diffused 'blurred' protein patterns with some protein material not entering the resolving gel. At 22°C there was some evidence of proteolysis but no evidence of high molecular weight polymer formation, while at 40°C both proteolysis and high molecular weight polymer formation increased with storage time. It appeared that both physico-chemical and proteolytic processes play some part in the mechanism of gelation in UHT reconstituted concentrated skim milk.     

High-pressure-induced interactions between milk fat globule membrane proteins and skim milk proteins in whole milk

The association of beta-lactoglobulin (beta-LG) and alpha-lactalbumin (alpha-LA) with milk fat globule membrane (MFGM), when whole milk was treated by high pressure in the range 100 to 800 MPa, was investigated using sodium dodecyl sulfate (SDS)-PAGE under reducing and nonreducing conditions. In SDS-PAGE under reducing conditions, beta-LG was observed in the MFGM material isolated from milk treated at 100 to 800 MPa for 30 min, and small amounts of alpha-LA and kappa-casein were also observed at pressures >600 MPa for 30 min. However, these proteins were not observed in SDS-PAGE under nonreducing conditions. These results indicate that beta-LG and alpha-LA associated with MFGM proteins via disulfide bonds during the high-pressure treatment of whole milk. The amount of beta-LG associated with the MFGM increased with an increase in pressure up to 800 MPa and with increasing time of pressure treatment. The maximum value for beta-LG association with the MFGM was approximately 0.75 mg/g of fat. Of the major original MFGM proteins, no change in butyrophilin was observed during the high-pressure treatment of whole milk, whereas xanthine oxidase was reduced to some extent beyond 400 MPa. In contrast to the behavior during heat treatment, PAS 6 and PAS 7 were stable during high-pressure treatment, and they remained associated with the MFGM.     

Comparison of casein micelles in raw and reconstituted skim milk

During the manufacture of skim milk powder, many important alterations to the casein micelles occur. This study investigates the nature and cause of these alterations and their reversibility upon reconstitution of the powders in water. Samples of skim milk and powder were taken at different stages of commercial production of low-, medium-, and high-heat powders. The nature and composition of the casein micelles were analyzed using a variety of analytical techniques including photon correlation spectroscopy, transmission electron microscopy, turbidity, and protein electrophoresis. It was found that during heat treatment, whey proteins are denatured and become attached to the casein micelles, resulting in larger micelles and more turbid milk. The extent of whey protein attachment to the micelles is directly related to the severity of the heat treatment. It also appeared that whey proteins denatured during heat treatment may continue to attach to casein micelles during water removal (evaporation and spray-drying). The process of water removal causes casein and Ca in the serum to become increasingly associated with the micelles. This results in much larger, denser micelles, increasing the turbidity while decreasing the viscosity of the milk. During reconstitution, the native equilibrium between colloidal Ca and serum Ca is slowly reestablished. The reequilibration of the caseins and detachment of the whey proteins occur even more slowly. The rate of reequilibration does not appear to be influenced by shear or temperature in the range of 4 to 40°C.     

Influence of thermosonication on Geobacillus stearothermophilus inactivation in skim milk

The influence of high intensity ultrasound coupled with thermoprocessing on the inactivation of Geobacillus stearothermophilus vegetative cells and spores in skim milk powder was explored using response surface methodology and two polynomial models were developed. Optimization of cell reduction (4.8 log) was found to be at 19.75% total solids (TS), 45 °C, and 30 s, while optimization of spore reduction (0.45 log) was found to be at 31.5% TS, 67.5 °C, and 17.5 s. Model verification experiments were performed using common milk powder processing conditions. Results showed the inactivation of cells and spores to be most effective before (9.2% TS, 75 °C, and 10 s) and after (50% TS, 60 °C, and 10 s) the evaporator during milk powder processing and may produce an additive effect in microbial reduction when the two locations are combined, resulting in a 5.8 log reduction for vegetative cells and 0.51 log reduction for spores.     

Microstructural changes in casein supramolecules during acidification of skim milk

Pasteurized skim milk was acidified using different levels of glucono-δ-lactone at 10, 20, 30, and 40°C to give slow, medium, and fast rates of acidification. Milk coagulation was monitored by measuring turbidity and curd firmness, and microstructural changes during acidification were observed on glutaraldehyde-fixed, agar-solidified milk samples using transmission electron microscopy. Rate of acidification had little influence on changes observed during acidification, except at 10°C. At 40°C, the casein supramolecules were spherical throughout acidification, whereas at lower temperatures they became progressively more ragged in appearance. All of the milks gelled at the same pH (pH 4.8), as measured by curd firmness, whereas increases in turbidity, assumed to be brought about by an increase in number of light-scattering particles, were observed to start at about pH 5.2 to 5.4. As the milk was acidified, aggregates of loosely entangled proteins were observed, presumably originating from proteins that had dissociated from the casein supramolecules. These aggregates were often as large as the casein supramolecules, particularly as the pH of the milk approached the isoelectric point of the caseins. Larger aggregates were observed at 40°C than at the lower temperatures, suggesting the involvement of hydrophobic interactions between the proteins. A 3-phase model for acid-induced gelation of milk is proposed in which the first phase involves temperature-dependent dissociation of proteins from the casein supramolecules, with more dissociation occurring as temperature is decreased. Dissociation continues as milk pH is lowered, with the released proteins forming into loosely entangled aggregates, some as large as the casein supramolecules. The second phase of acid gelation of milk occurs between pH 5.3 and pH 4.9 and involves a reassociation of proteins with loosely entangled protein aggregates forming into more-compact colloidal particles or combining with any remaining casein supramolecules. The third and final phase involves rapid aggregation of the colloidal casein supramolecules into a gel network at about pH 4.8. Different gel structures were formed based on temperature of acidification, with a coarse-stranded gel network formed at 40°C and a fine-stranded gel network at 10°C.     

The nutritional value of dried skim milk in broiler diets

Two experiments are reported in which dried skim milk was used at levels of 0, 40, 80, 120 and 160 g kg^?1 of diet to replace mainly fishmeal in broiler diets. In experiments 1 and 2, the stocking densities were 0.2 and 0.08 m² per bird, respectively. Food intake was increased by dried skim milk, particularly at the higher levels of inclusion. Live-weight gain was not affected by the inclusion of skim milk, but the efficiency of food conversion was adversely affected after week 1 in experiment 1 and by week 4 in experiment 2. Litter moisture content was virtually unaffected by treatment in experiment 1 but was significantly increased by dietary treatment in experiment 2. It is suggested that the wet litter had contributed to the incidence of breast-burn in the broilers.     

Effect of lactose content on dielectric properties of whole milk and skim milk

Dielectric properties (dielectric constant ε′ and dielectric loss factor ε′′) of whole milk and skim milk with the lactose content of 4.56–6.44% and 4.57–6.47%, respectively, were measured over the frequency range of 20–4500 MHz at 25 °C using a vector network analyzer. The results showed that ε′ decreased with increasing frequency, and ε′′ changed with V shape and its minimum was noted at about 2000 MHz. Whole milk had lower dielectric properties than skim milk at almost same lactose content and a given frequency. ε′ had weak positive linear relationship with lactose content for whole milk, but had negative linear relationship for skim milk. No matter for which milk, ε′′ had very good negative linear relationship with lactose content below 1000 MHz and had good positive linear relationship above 2300 MHz. The study provides information on developing rapid lactose detector for milk in future.     

Lactosylation of milk proteins during the manufacture and storage of skim milk powders

Extensive lactosylation of milk proteins in standard skim milk powder dried against air between 185 and 90°C (inlet and outlet temperatures of the air) was detected by capillary electrophoresis. Optimisation of the drying conditions included keeping the outlet temperature low (preferably <80°C), since this was the parameter which most affected the extent of lactosylation of milk proteins. The inlet temperature was set in order to obtain the best compromise between a low extent of lactosylation and a high drying rate (170–175°C). These conditions allowed the manufacture of low-lactosylated skim milk powder. Storage of freeze-dried and control low-lactosylated skim milk powder at different temperatures showed that both temperature and moisture content affected the progress of lactosylation during storage. Further drying to less than 2.5% moisture content (w/w) and storage at low temperatures were required to prevent the development of lactosylation in the low-lactosylated skim milk powder.     

Effect of beta-lactoglobulin A and B whey protein variants on the rennet-induced gelation of skim milk gels in a model reconstituted skim milk system

The effect of fortifying reconstituted skim milk with increasing levels of the β-lactoglobulin (β-LG) genetic variants A, B, and an A-B mixture on rennet-induced gelation was studied by small deformation-sensitive rheology. Free-zone capillary electrophoresis and high-sensitivity oscillatory rheology were used to elucidate the role of potential heterotypic associative interactions between whey proteins and casein in a mixed colloidal system, subjected to moderate heating (65°C for 30 min) prior to renneting, on the gelling properties of the system. Increasing levels of added whey protein, in the concentration range of 0.225 to 1.35% of added protein, led to a concomitant progressive increase in the equilibrium shear storage modulus, G′ (recorded after ∼10,800 s), in the order β-LG B > β-LG A and β-LG A-B, as the general expected consequence of the setup of denser casein gel networks. The preferential effect of β-LG B over β-LG A on the mechanical strength of the gels may be due to the formation of cross-links and aggregates involving whey proteins and rennet hydrolysis products or an increase in the size of the casein micelle caused by the grafting of β-LG B to its surface, or both. The results of free-zone capillary electrophoresis were consistent with the notion that β-LG B (and not β-LG A) binds to the casein micelle under an optimal stoichiometry of 1:0.045 (mg/mg), even in the absence of heat treatment. The liquid-like character of the gel networks formed, tan δ, was a parameter sensitive to the level of addition of β-LG A in particular. At low concentrations (up to 0.45%) of β-LG A, tan δ increased by almost twice as much, which was interpreted as a result of the increase in the loss modulus, G″, of the sol fraction because of the presence of unbound β-LG A. At greater incremental concentrations of β-LG (>0.45%), the formation of smaller whey protein aggregates confined to the sol fraction may have led to a progressive decrease in tan δ. The critical gel time, t_gel, was also affected by the concentration of added whey protein and described 3 zones of behavior, irrespective of the type of whey protein variant. The critical gel time was slightly shorter for β-LG B than for β-LG A at 0.45% of added whey protein, but this difference became larger at 0.67%. Even when only β-LG B was found to associate with casein prior to renneting, both β-LG A and β-LG B, either alone or mixed, had a profound influence on the mechanical strength and coagulation kinetics of the rennet-induced casein gels. This knowledge is expected to be useful to exert better control and optimize processing conditions during the manufacturing of cheese and cheese analogs.