Biomedical subjects

R Jiménez-Flores

Publications and source records attributed to R Jiménez-Flores.

16 recordsLinked to original sources

PubMed2006

Compositional and functional properties of buttermilk: a comparison between sweet, sour, and whey buttermilk.

Buttermilk is a dairy ingredient widely used in the food industry because of its emulsifying capacity and its positive impact on flavor. Commercial buttermilk is sweet buttermilk, a by-product from churning sweet cream into butter. However, other sources of buttermilk exist, including cultured and whey buttermilk obtained from churning of cultured cream and whey cream, respectively. The compositional and functional properties (protein solubility, viscosity, emulsifying and foaming properties) of sweet, sour, and whey buttermilk were determined at different pH levels and compared with those of skim milk and whey. Composition of sweet and cultured buttermilk was similar to skim milk, and composition of whey buttermilk was similar to whey, with the exception of fat content, which was higher in buttermilk than in skim milk or whey (6 to 20% vs. 0.3 to 0.4%). Functional properties of whey buttermilk were independent of pH, whereas sweet and cultured buttermilk exhibited lower protein solubility and emulsifying properties as well as a higher viscosity at low pH (pH <or= 5). Sweet, sour, and whey buttermilks showed higher emulsifying properties and lower foaming capacity than milk and whey because of the presence of milk fat globule membrane components. Furthermore, among the various buttermilks, whey buttermilk was the one showing the highest emulsifying properties and the lowest foaming capacity. This could be due to a higher ratio of phospholipids to protein in whey buttermilk compared with cultured or sweet buttermilk. Whey buttermilk appears to be a promising and unique ingredient in the formulation of low pH foods.

Animals↗

PubMed2006

Sensory, functional, and analytical comparisons of whey butter with other butters.

The objective of this work was to characterize the sensory attributes of whey (WB), cultured (CB), and regular sweet cream (SB) unsalted butters produced at the Dairy Products Technology Center (experimental; n = 3) or obtained from commercial sources (n = 6). Nine judges were trained for nine 1-h sessions; they then rated samples on a 15-cm line scale in triplicate using descriptive analysis. Data obtained were analyzed using SAS statistical software. Significant differences between the 3 types of butters were obtained on yellow, shiny, acidic odor, melt rate, porous, hard, spreadable, cheese odor, mouthcoating, nutty, cardboard odors, acidic, nutty, diacetyl, and grassy flavors. Cultured butter and SB were significantly shinier than WB. Whey butter was more yellow than CB, which in turn was more yellow than SB. Whey butter was more porous, and had higher scores on nutty flavor and cardboard odor than SB and CB. Sweet cream butter was significantly harder than CB but not WB. Cultured butter had more mouthcoating, acidic odor and flavor, and grassy flavor than SB and WB. The commercial samples were more porous, crumbly, and had significantly more artificial butter odor, rancid odor, and flavor. Results from principal component analysis indicated that experimental WB and SB were similar and were characterized by a sweet taste. Whey butter's characteristics compared favorably with commercial CB and were very similar to sweet cream butter. No major significant differences were obtained for triangle tests, with the exception of that for WB and CB in pound cake. No significant differences were obtained for the acceptability of the different versions of any of the 3 foods.

Butter↗

PubMed2006

Sensory evaluation of whey and sweet cream buttermilk.

The objective of this work was to characterize the sensory attributes of sweet cream buttermilk (CBM) and a nontraditional product, whey buttermilk (WBM). Whey buttermilk results from processing whey cream into butter. The products were evaluated as fresh liquid buttermilk obtained directly from the butter churn, and as reconstituted buttermilk or whey buttermilk powders. Sweet cream buttermilk and WBM were produced either at the Dairy Products Technology Center (experimental samples, n = 2) or provided by the industry (n = 2 from 2 different commercial sources). Nine panelists were trained for twenty-four 1-h sessions; they then rated samples on a 15-cm line scale in triplicate using descriptive analysis. Data obtained were analyzed using SAS statistical software. Results indicated that WBM had similar sensory characteristics as regular CBM; however, there was a marked color difference between them. Liquid buttermilk was not significantly different from reconstituted buttermilk powder on many attributes. However, WBM was significantly more yellow, more sour, and more astringent than the CBM samples, and it had more cardboard flavor than the commercially produced CBM. Liquid buttermilk was not significantly different from reconstituted buttermilk powder on many attributes. However, some buttermilk types had more cardboard aroma and flavor in their powdered form than in liquid form. Most attributes showed no significant differences across replicates, indicating consistency of rating. Principal component analysis showed that attributes were separated on the 2 principal components based on production site and processing form (fresh vs. reconstituted).

Adult↗

PubMed2004

Effect of temperature and pore size on the fractionation of fresh and reconstituted buttermilk by microfiltration.

The objective of this research was to evaluate the effect of temperature (7, 25, and 50 degrees C) and pore size (0.1, 0.8, and 1.4 micro m) on the separation of proteins and lipids (neutral lipids and phospholipids) during microfiltration (MF) of fresh or reconstituted buttermilk. Buttermilk was subjected to MF using a pilot-scale unit mounted with ceramic membranes. The MF runs were carried out in a uniform transmembrane pressure (UTP) mode. Changes in processing temperature had no significant impact on protein transmission, whereas increasing temperature reduced both lipid and phospholipid transmission. A maximum concentration factor (CF) for lipids was reached at 25 degrees C, as protein CF remained essentially unaffected by temperature. The use of the smaller pore size (0.1 microm) resulted in low lipid (10%) and protein (approximately 20%) transmission. Larger pore sizes (0.8 and 1.4 microm) resulted in higher levels of protein, lipid, and phospholipid transmission (>50%), but gave high permeation fluxes. Transmission of both proteins and lipids was markedly different when using fresh buttermilk as opposed to reconstituted buttermilk. This study showed that MF temperature, pore size, and buttermilk type influence fractionation but that MF alone cannot achieve optimal separation of lipids and proteins for the production of novel ingredients from buttermilk.

Chemical Fractionation↗

PubMed2004

Effect of genetic variation on the tryptic hydrolysis of bovine beta-lactoglobulin A, B, and C.

The structure, stability, and hydrolysis characteristics of beta-lactoglobulin (LG) A are different from those of either beta-LG B or beta-LG C. Purified samples of these proteins were hydrolyzed with trypsin and the rates of loss of native monomeric beta-LG structure were measured using sodium dodecyl sulfate PAGE. At the same time, the appearance of many individual peptides were identified and followed in time by HPLC, measuring their concentration as a function of solution pH, temperature, protein concentration, and added urea or palmitate. The identity of the peptides was confirmed by liquid chromatography-mass spectrometry. This semiquantitative exploration showed that the rate of hydrolysis was in the order beta-LG A > beta-LG B > beta-LG C under most circumstances, and that 12 of the 18 trypsin-susceptible bonds were cleaved at very similar rates that were governed by the variant type. Consequently, the rate of hydrolysis of the intact protein was related to the overall structural stability of the individual proteins and the accessibility of certain peptide bonds to the enzyme. The hydrolysis of mixtures of 2 or more variants or of denatured beta-LG gave more heterogeneous peptide mixtures.

Animals↗

PubMed2003

Concentration of polar MFGM lipids from buttermilk by microfiltration and supercritical fluid extraction.

Buttermilk contains the milk fat globule membrane (MFGM), a material that possesses many complex lipids that function as nutritionally valuable molecules. Milk-derived sphingolipids and phospholipids affect numerous cell functions, including regulating growth and development, molecular transport systems, stress responses, cross membrane trafficking, and absorption processes. We developed a two-step method to produce buttermilk derivative ingredients containing increased concentrations of the polar MFGM lipids by microfiltration and supercritical fluid extraction (SFE). These processes offer environmentally benign alternatives to conventional lipid fractionation methods that rely on toxic solvents. Firstly, using a ceramic tubular membrane with 0.8-micron pore size, we evaluated the cross flow microfiltration system that maximally concentrated the polar MFGM lipids using a 2n factorial design; the experimental factors were buttermilk source (fresh, or reconstituted from powder) and temperature (50 degrees C, and 4 degrees C). Secondly, a SFE process using supercritical carbon dioxide removed exclusively nonpolar lipid material from the microfiltered buttermilk product. Lipid analysis showed that after SFE, the product contained a significantly reduced concentration of nonpolar lipids, and a significantly increased concentration of polar lipids derived from the MFGM. Particle size analysis revealed an impact of SFE on the product structure. The efficiency of the SFE system using the microfiltration-processed powder was compared much more favorably to using buttermilk powder.

Animals↗

PubMed2003

Rheological properties of concentrated skim milk: importance of soluble minerals in the changes in viscosity during storage.

Properties of condensed milks prior to spray drying dictate to a large extent the functionality of the resulting milk powder. Rheological properties of concentrated skim milk, with total solids content of 45% but different mineral content, were studied as a function of shear rate and storage time at 50 degrees C. These milks are proposed as a model to study the effects of minerals on rheology and age gellation of condensed milk prior to drying. During storage of the concentrated milk, the apparent viscosity, particularly after 4 h, increased markedly at all shear rates studied. The yield stress also increased steeply after 4 h of storage at 50 degrees C. The changes in apparent viscosity of concentrated milk stored for up to 4 h were largely reversible under high shear, but irreversible in samples stored for longer time. The appearance of yield stress suggested the presence of reversible flocculation arising from weak attraction between casein micelles, with a transition from reversible to irreversible aggregation during storage. Particle size analysis confirmed irreversible aggregation and fusion of casein micelles during storage. Gradual reduction of mineral content of concentrated milks resulted in a marked decrease in the apparent viscosity and casein micelle aggregation during storage, while addition of minerals to milk had the opposite effect. The results demonstrated that the soluble mineral content is very important in controlling the storage-induced changes in the rheology of concentrated milks.

Animals↗

PubMed2002

Scale-up of native beta-lactoglobulin affinity separation process.

Affinity separation of beta-lactoglobulin in its native form with all-trans-retinal immobilized on calcium bio-silicate was scaled up and applied to separate it from industrial sweet whey. Three different methods of mixing the modified calcium bio-silicate and whey for the interaction between all-trans-retinal and beta-lactoglobulin were tried at pilot scale. The three methods used were 1) a column packed with calcium bio-silicate, 2) a stirred tank, and 3) a fluidized bed column of calcium bio-silicate particles. Adsorption and desorption of beta-lactoglobulin were carried out at pH 5.1 and 7.0, using 0.01 and 0.1 M phosphate buffers, respectively. The phosphate buffer containing desorbed beta-lactoglobulin was concentrated 20 times using ultrafiltration and then freeze-dried. The packed column, stirred tank, and fluidized bed column produced beta-lactoglobulin with purity of 80, >95, and >95%, and recovery of 0.65, 2.88, and 2.88 g per kilogram of calcium bio-silicate, respectively. The comparative poor purity and recovery of beta-lactoglobulin in the case of the packed column was attributed to insufficient contact between the passing fluids and the calcium bio-silicate during adsorption, desorption, and intermittent washing. The fluidized bed column method, with a gentle mixing action, was considered the best suited for further scale up to the industrial level.

Adsorption↗

PubMed2002

Rapid simultaneous determination of organic acids, free amino acids, and lactose in cheese by capillary electrophoresis.

A capillary electrophoresis (CE) method for the simultaneous separation of 11 metabolically important organic acids (oxalic, formic, citric, succinic, orotic, uric, acetic, pyruvic, propionic, lactic, and butyric), 10 amino acids (Asp, Glu, Tyr, Gly, Ala, Ser, Leu, Phe, Lys, and Trp), and lactose has been optimized, validated, and tested in dairy products. Repeatability and linearity were calculated for each compound, with detection limit values as low as 0.2 x 10(-2) mM for citric acid and Gly. The method was applied to analyze yogurt and different varieties of commercial cheeses. This method yielded specific CE patterns for different varieties of cheese. Also, it has been shown to be sensitive enough to measure small changes in composition of some of those compounds in fresh cheese stored under accelerated ripening conditions for 2 d at 32 degrees C (e.g., from 1728.3 +/- 45.0 to 1166.7 +/- 4.5 mg/100 g of DM in the case of lactose, or from 23.5 +/- 0.6 to 76.8 +/- 16.7 mg/100 g of DM in the case of acetic acid).

Acetic Acid↗

PubMed2001

Expression and purification of glycosylated bovine beta-casein (L70S/P71S) in Pichia pastoris.

Post-translational glycosylation of bovine beta-casein (L70S/P71S) that results in Asn(68)-linked glycan on the protein was obtained in up to 30% of total beta-casein expressed in the methylotrophic yeast Pichia pastoris. Among the growth/induction media used, buffered minimal glycerol (BMG)/buffered minimal methanol (BMM) media were best for the production of glycosylated bovine beta-casein, indicating pH-dependent glycosylation. Glycosylated bovine beta-casein (L70S/P71S) expressed in P. pastoris was purified to homogeneity by the combination of ammonium sulfate fractionation, Concanavalin A--Sepharose affinity column, and Mono Q anion-exchange FPLC. The purified glycosylated bovine beta-casein was specific only to Concanavalin A, and the oligosaccharide structure of glycosylated beta-casein was of high-mannose type. Unlike the hyperglycosylation that occurred in yeast, the majority of bovine beta-casein was not hyperglycosylated in P. pastoris, and its molecular weight was estimated to be 33.6 kDa. Glycosylated bovine beta-casein was normally phosphorylated to the same degree as native bovine beta-casein.

Animals↗

PubMed1997

Trends in research for alternate uses of milk fat.

During the past 2 yr, sales of butter have increased, and the inventory of milk fat in the US has decreased. However, still fresh in memory are the large inventories of butter and low prices for milk fat. Although economic peaks and valleys are a result of consumer preferences, research in the area of milk lipids is very active. This paper is a limited review of the continuing research trends and technological advances in the field of lipids, particularly milk fat. The modification of milk fat composition through cattle nutrition, fractionation by melt crystallization and supercritical fluid extraction, blending, interesterification, and glycerolysis as well as the emerging importance of analysis of lipids are some of the areas for which active research promises future advances in milk fat technology.

Animals↗

PubMed1997

Characterization and partial purification of bovine alpha-lactalbumin and beta-casein produced in milk of transgenic mice.

Bovine alpha-lactalbumin (alpha-LA) and bovine beta-casein (beta-CN), from milk from transgenic mice were characterized and partially purified using electrophoretic, immunoblotting, and chromatographic methods. The transgenically expressed bovine milk proteins were identified using PAGE or by a combination of preparative isoelectrofocusing followed by Western immunoblotting. The heterologous bovine alpha-IA and bovine beta-CN had molecular masses that were identical to those of those of the native proteins. The estimated expression of the proteins was 1.0 mg/ml of milk for alpha-LA and 3.0 mg/ml for beta-CN. The calcium binding of bovine alpha-LA suggested that the protein produced in murine milk has the same electrophoretic shift as native bovine alpha-LA after the removal of calcium. Nitrogen-linked glycosylation of native and murine synthesized bovine alpha-LA was identified by peptide-N-glycosidase F treatment, and the N-terminal amino acid sequence of HPLC-purified bovine alpha-LA from mouse milk was confirmed to be identical to native bovine alpha-LA. In addition, the phosphorylation of the bovine beta-CN expressed in the milk of transgenic mice was the same as that of native bovine beta-CN, as determined by phosphatase digestion.

Amino Acid Sequence↗

PubMed1996

Expression of a bovine kappa-CN cDNA in the mammary gland of transgenic mice utilizing a genomic milk protein gene as an expression cassette.

Transgenic mice were produced by microinjection of a DNA construct composed of the bovine kappa-casein (kappa-CN) cDNA under the control of the goat beta-CN 5' promoter elements and 3' flanking regions into pronuclear-stage embryos. The gene construct targeted the expression of bovine kappa-CN RNA to the mammary gland and secretion of bovine kappa-CN in the milk. In the three lines studied (BC-7, BC-31 and BC-67) the transgene was stably integrated and propagated as a Mendelian locus. Expression of the bovine protein in lactating mice from the three transgenic lines was demonstrated by northern and western blots. In ten different tissues analysed by northern blotting, expression was confined to the mammary gland of lactating transgenic mice from line BC-7, with low-level expression also observed in the salivary gland of lines BC-31 and BC-67. Transgene expression in the mammary gland paralleled normal casein gene expression during lactation and was not observed in virgin females. The level of bovine kappa-CN mRNA expression on day 10 of lactation in hemizygous transgenic females in relation to endogenous mRNA of whey acid protein (WAP) gene expression was 14%, 69%, and 127% in lines BC-7, BC-31 and BC-67, respectively. No association between transgene copy number and expression was observed. The bovine kappa-CN concentration in milk on day 10 of lactation ranged from 0.94 to 3.85 mg of protein per ml of milk. The bovine kappa-CN expressed in mouse milk had the same molecular mass and immunoactivity with polyclonal antibodies as did kappa-CN from bovine milk. A high degree of variation in the production of bovine kappa-CN within each of the transgenic lines was observed.

Amino Acid Sequence↗

PubMed1995

DNA sequence of the porcine alpha-lactalbumin 5' flanking region and single-base polymorphisms within this region.

The 5' flanking region of the alpha-lactalbumin (alpha-LA) gene was sequenced for the Duroc, Yorkshire and Meishan breeds of swine to identify potential sequence variants within this regulatory region of the porcine alpha-LA gene. The sequenced region of the gene encompasses 391bp5' of the translation start site to 11bp3' of the translation start site. Within this sequence of the porcine alpha-LA gene two single-base pair differences were detected. One variant occurs at position -178 and the other at position -235 from the translation start site. Each of the variations can be detected by a restriction fragment length polymorphism within a polymerase chain reaction amplified product. The polymorphisms at the -178 and -235 positions appear to be genetically linked in the animals that have been analysed.

Animals↗

PubMed1994

Insulin-like growth factors and insulin-like growth factor binding proteins in porcine serum and milk throughout lactation.

IGF-I, IGF-II, and IGF binding proteins (IGFBP) were characterized in porcine serum, colostrum, and milk on d 1-28 postpartum. IGF-I and -II were measured by heterologous RIA. Serum IGFBP were characterized by Western ligand blotting and milk IGF binding activity by [125I]-IGF binding assay. IGF-II accounted for 70-85% of serum IGF and rose 2-fold between d 1 and d 28. Serum IGF-I was unaffected by duration of lactation. Milk IGF-II concentrations were higher than IGF-I concentrations on d 1-7 postpartum. After d 10, milk IGF-I and IGF-II contents were not significantly different. Serum contained IGFBP with M(r) of 43, 39, 34, 28, and 24 kD. Over the course of lactation, the 43- and 39-kD bands increased, the 24-kD band decreased, and the 34- and 28-kD bands were unchanged. Milk IGF binding activity increased between d 1 (28%) and d 3 (44%), then declined until d 28 (7%). Serum and milk were separated by isoelectric focusing into 20 fractions, across a gradient from pH 3 to 10, that were screened for IGFBP by Western ligand blotting. Milk contained six IGFBP of similar M(r) as serum IGFBP; however, the relative amounts of the IGFBP and their apparent isoelectric points differed. In conclusion, porcine milk contains both IGF-I and -II, with IGF-II predominating. Several IGFBP with similar M(r) as those found in serum are present in milk. IGF peptide concentrations were highest in prepartum secretions and colostrum, whereas IGF binding activity peaked on d 4 of lactation.

Animals↗

PubMed1994

Two-dimensional electrophoretic analysis of proteins of bovine mammary gland secretions collected during the dry period.

Proteins in mammary gland secretions, collected from Holstein cows during the dry period, were analyzed by preparative isoelectric focusing, followed by SDS-PAGE. Protein profiles changed throughout the dry period. Intact casein bands were present throughout the dry period, but in reduced proportions from d 7 after dry-off through d 7 prepartum. Breakdown fragments of casein were particularly apparent in secretions from d 7 to 21 of the dry period. A fragment of beta-CN (approximately 13 kDa) was identified in secretions collected on d -1 prior to dry-off through d 21 of the dry period. beta-Lactoglobulin generally focused in a limited number of fractions, but, in the sample at d 21 prepartum, beta-LG focused over a broad pH range. Lactoferrin was found in all fractions after isoelectric focusing, but specific degradation products of lactoferrin were apparent only at certain times during the dry period. This method is a valuable approach for separation of proteins from the complex mixtures found in mammary secretions during the dry period. A number of peptides identified by this method may be generated from breakdown of milk proteins in the mammary gland during the dry period and could have a role in the involuting gland.

Amino Acid Sequence↗