Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “PECTINS”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 109 records · Page 6Linked to original sources

Interactions between beta-lactoglobulin and pectins during in vitro gastric hydrolysis.

This paper deals with the influence of different levels of three pectins, low-methylated pectin (LMP), high-methylated pectin (HMP), and low-methylated and amidated pectin (LMA), on the in vitro gastric hydrolysis of beta-lactoglobulin (beta-lg). Proteolysis by pepsin consisted of a 2-h progressive reduction of pH. A turbidity measurement of beta-lg-pectin mixtures was carried out during the proteolysis. The influence of pectins on pepsin enzymatic activity was also evaluated. beta-Lg was resistant to peptic digestion. The presence of each of the three pectins at a concentration of 50 wt % increased the N release at all pH values considered, despite a significant inhibition of the pepsin enzymatic activity with the pectins. The turbidity of beta-lg solutions during proteolysis was reduced by the addition of pectins, because of the formation of electrostatic complexes between this protein and pectins. The increase of N release could be a false positive result due to the difficulty of precipitating protein by trichloroacetic acid because of the formation of electrostatic complexes demonstrated by the decrease of turbidity.

Hydrogen-Ion Concentration↗

Identification of a bacterial pectin acetyl esterase in Erwinia chrysanthemi 3937.

Erwinia chrysanthemi causes soft-rot diseases of various plants by enzymatic degradation of the pectin in plant cell walls. The structural complexity of pectin requires the combined action of several pectinases for its efficient breakdown. Three types of pectinases have so far been identified in E. chrysanthemi: two pectin methyl esterases (PemA, PemB), a polygalacturonase (PehX), and eight pectate lyases (PelA, PelB, PelC, PelD, PelE, PelL, PelZ, PelX). We report in this paper the analysis of a novel enzyme, the pectin acetyl esterase encoded by the paeY gene. No bacterial form of pectin acetyl esterases has been described previously, while plant tissues and some pectinolytic fungi were found to produce similar enzymes. The paeY gene is present in a cluster of five pectinase-encoding genes, pelA-pelE-pelD-paeY-pemA. The paeY open reading frame is 1650 bases long and encodes a 551-residue precursor protein of 60704Da, including a 25-amino-acid signal peptide. PaeY shares one region of homology with a rhamnogalacturonan acetyl esterase of Aspergillus aculeatus. To characterize the enzyme, the paeY gene was overexpressed and its protein product was purified. PaeY releases acetate from sugar-beet pectin and from various synthetic substrates. Moreover, the enzyme was shown to act in synergy with other pectinases. The de-esterification rate by PaeY increased after previous demethylation of the pectins by PemA and after depolymerization of the pectin by pectate lyases. In addition, the degradation of sugar-beet pectin by pectate lyases is favoured after the removal of methyl and acetyl groups by PemA and PaeY, respectively. The paeY gene was first identified on the basis of its regulation, which shares several characteristics with that of other pectinases. Analysis of the paeY transcription, using gene fusions, revealed that it is induced by pectic catabolic products and is affected by growth phase, oxygen limitation and catabolite repression. Regulation of paeY expression appears to be dependent on the KdgR repressor, which controls all the steps of pectin catabolism, and on the catabolite regulatory protein (CRP), the global activator of sugar catabolism. The contiguous pelD, paeY and pemA genes are transcribed as an operon from a promoter proximal to pelD which allows the regulation by KdgR and CRP. However, transcription can be interrupted at the intra-operon Rho-independent terminator situated between pelD and paeY. The paeY mutant inoculated into Saintpaulia plants was less invasive than the wild-type E. chrysanthemi strain 3937, demonstrating the important role of PaeY in the soft-rot disease.

Acetylation↗

Colonic drug delivery: influence of cross-linking agent on pectin beads properties and role of the shell capsule type.

For colonic delivery, pectin beads obtained by ionotropic gelation method have been already reported as an interesting approach. This study investigated the influence of the cross-linking agent (calcium or zinc) and the type of shell capsule used (classical or enteric capsules) on pectin beads properties and on their performance to target the colon (in vitro dissolution studies with subsequent pH change to mimic overall gastro-intestinal tract). Zinc pectinate beads seemed to be relatively similar to calcium's ones in morphological point, except on the surface aspect. When beads were introduced in classical hard capsules, ketoprofen release was not significantly different between CPG and ZPG beads, and it was too premature and too quick due to a chemical erosion of the pectinate matrix (acid + basic attacks). However, zinc pectinate beads showed slower ketoprofen release compared with calcium pectinate beads when enteric hard capsules were used. This interesting finding could be due to the strength of the network formed during the process between the zinc cations and the LM-pectin following the "egg-box" model. This network was stronger and induced a reduction of swelling and hydration when contact with dissolution medium, then subsequently a decrease of drug release. Thus, the zinc pectinate beads could protect sufficiently drug entrapped from the upper gastro-intestinal conditions and drug release will be controlled by pectin degradation with colonic microflora. Finally, these zinc pectinate beads in enteric hard capsules are promising as a carrier for specific colonic delivery of drugs after oral administration.

Administration, Oral↗

Effects of apple pectin on fecal bacterial enzymes in azoxymethane-induced rat colon carcinogenesis.

Because of the potential significance of colonic bacteria in colon carcinogenesis, we investigated the effect of pectin of different types on fecal bacterial enzymes (beta-glucuronidase, beta-glucosidase and tryptophanase) at various periods of time after feeding rats with pectin-containing diets during azoxymethane-induced colon carcinogenesis. The diet supplemented with 20% apple pectin or 20% citrus pectin decreased the multiplicity of colon tumors, and the number of tumors was significantly decreased in the group fed apple pectin. The incidence of colon tumors in the apple pectin group was lower than that in the control group. The mean tumor size was similar among the three groups. Apple pectin feeding decreased fecal beta-glucosidase and tryptophanase levels. Furthermore, a significant decrease in the activity of beta-glucuronidase was observed in the apple pectin group during the initiation phase. These findings suggest that the protective effect of pectin on colon carcinogenesis may be dependent on the type of pectin and be related to the decrease of beta-glucuronidase activity in the initiation stage of carcinogenesis.

Adenocarcinoma↗

Inhibition of atherosclerosis by dietary pectin in microswine with sustained hypercholesterolemia.

Sustained hypercholesterolemia is a known risk factor for development of atherosclerosis. In animal studies, grapefruit pectin fed concurrently with a high-lipid diet inhibits hypercholesterolemia and atherogenesis. The purpose of the present study was to determine if grapefruit pectin affects cholesterol levels and atherogenesis of animals with established hypercholesterolemia. Microswine were fed an atherogenic diet to establish hypercholesterolemia. Plasma cholesterol levels rose rapidly and for 360 days were sustained at levels 6- to 12-fold the normal level. Then, half the microswine, selected at random, were fed a diet in which 3% grapefruit pectin was substituted for cellulose, and the remaining animals received the original diet. Animals were killed 270 days later, and the extent of atherosclerosis was determined. In animals with established hypercholesterolemia, pectin did not lower their cholesterol levels. However, pectin reduced the extent of atherosclerosis in both the aorta and coronary arteries. The mean surface area covered by atherosclerosis in the aorta was 13.6% in the group that did not receive pectin compared with 5.3% in the group that did receive pectin. The mean coronary artery narrowing was 45% without pectin and 24% with pectin. We conclude that pectin may have a direct beneficial effect on atherosclerosis by a mechanism independent of cholesterol levels.

Animals↗

Effects of pelleting, lactose level, polyethylene glycol 4000, and guar gum compared to pectin on growth performances, energy values, and losses of lactose, lactic acid, and water in chickens.

Five mash and two pelleted diets were tested in broiler chickens (7 to 19 d). Mash diets consisted of a basal fraction diluted with either .5% pectin or .5% guar gum. Mash pectin and guar gum diets contained either 3% lactose (PL3m and GL3m diets, respectively) or 6% lactose (PL6m and GL6m diets, respectively). Compositions of pelleted diets (PL3p and GL3p) were those of PL3m and GL3m diets, respectively. All diets contained .5% polyethylene glycol 4000 (PEG) except the PL3m0 diet. The latter diet differed from PL3m diet by the PEG content, only. The real applied viscosities of pectin and guar gum diets were 1.48 and 4.94 mL/g, respectively, No effect of PEG was detected on growth performances, and excreta losses of lactose, lactic acid, and water. No negative effect of guar gum compared to pectin was observed on body weight (19 d), except with pelleted diets (P < .05). Feed:gain ratios for guar gum diets were 7% higher (P < or = .001) that those of pectin diets. The AMEn values of guar gum diets were 4% lower (P < or = .001) than those of pectin diets. For mash diets, lactose digestibilities were lower (P < .05) with guar gum than with pectin. Increasing lactose level from 3 to 6% did not affect (P > .05) AMEn values, feed: gain ratios, and body weights (19 d) but reduced (P > .001) lactose digestibilities from 78 to 64%. The positive effects of pelleting on body weights (19 d) were much less pronounced with guar gum than with pectin (P < .05). The AMEn values of pelleted diets (PL3p) and GL3p) were, on average, 2.5% lower (P = .005) than their mash counterparts (PL3m and GL3m). Water losses related to feed intake were greater with guar gum than with pectin (P < .001) and with 6% lactose than with 3% (P = .001) but were not affected (P > .05) by pelleting. Lactic acid losses related to feed intake were increased by guar gum compared with pectin (P < .001), with more pronounced effects induced by high lactose level (P < .05) and pelleting (P < .05). In many respects, the effects of guar gum seemed similar to those observed in an acid liquid diarrhea.

Animal Feed↗

Pectin-enriched diet affects distribution and expression of apoptosis-cascade proteins in colonic crypts of dimethylhydrazine-treated rats.

The colonic crypt contains highly proliferative cells in its base and differentiated cells on its luminal surface. Carcinogenesis significantly affects this orderly cellular distribution. The aims of this study were: i) to examine the expression of apoptosis-related proteins along the crypt-lumen axis during 1, 2-dimethylhydrazine (DMH)-induced carcinogenesis, ii) to assess whether a diet supplemented with the soluble fiber pectin affects those parameters, in comparison to non-carcinogen-treated rats and in relation to rats fed a standard diet and treated with DMH. The pectin-enriched diet induced upregulation of active caspase-1 subunit (20 kDa) and of caspase-3 precursor in DMH-treated rats. Pectin enhanced caspase-3 activity in all colonocyte populations, in both non-DMH and DMH-treated rats. The luminal colonocytes exhibited higher caspase-3 activity than proliferative colonocytes of rats fed a standard diet in non-DMH and DMH-treated rats, whereas in pectin-fed non-DMH-treated rats, equal activity was measured among all colonocyte populations. In the DMH-treated rats, the cleaved poly(ADP-ribose) polymerase subunit (89 kDa) was detected in luminal colonocytes of rats fed pectin and was higher than in rats fed the standard diet. Bak was equally expressed in isolated colonocytes from rats of both dietary groups treated with DMH and in the normal rats fed pectin, whereas in the non-DMH-treated rats fed a standard diet, higher expression was obtained in differentiated colonocytes. In the DMH-treated rats, Bcl-2 expression was lower in all colonocytes harvested from rats fed pectin, relative to rats fed the standard diet. Apoptotic index in the DMH-treated groups was higher in rats receiving the pectin diet compared with the standard diet in both the differentiated cell populations and the proliferating colonocytes. Average tumor number and volume per rat were lower in rats fed pectin. These findings indicate that dietary fibers regulate expression, function and distribution of apoptotic-related proteins in the crypt during colon carcinogenesis, changes that probably induce a reduction in tumor volume. We assume that butyrate, produced following fermentation of pectin, may play a key role in these effects.

1,2-Dimethylhydrazine↗

Anticarcinogenic action of apple pectin on fecal enzyme activities and mucosal or portal prostaglandin E2 levels in experimental rat colon carcinogenesis.

Pectin is a partially methoxylated polymer of galacturonic acid obtained from fruits. Among pectin, apple pectin exerts stronger bacteriostatical action on Staphylococcus aureus, Streptococcus faecalis, Pseudomonas aeruginosa and Escherichia coli in comparison with citrus pectin. In this study, we used water-soluble methoxylated pectin from apple. The diet, supplemented by 20% apple pectin, significantly decreased the number of tumors and the incidence of colon tumor. PGE2 level in distal colonic mucosa in 20% apple pectin fed rats were lower than those in basal diet fed rats. Fecal beta-glucuronidase activities in the apple pectin fed group, which has been considered a key enzyme for the final activation of Dimethylhydrazine metabolism to carcinogens in the colonic lumen, were signifieantly lower than those in control group at initiation stage of carcinogenesis. In the case the concentrations of beta-glueosidase and azoreductase were also decreased. The effect of apple pectin on the colon carcinogenesis may partially depend on PGE, concentration decrease in colonic mucosa and on the type of pectin, also related to fecal enzyme activities.

Animals↗

Encapsulated Escherichia coli in alginate beads capable of secreting a heterologous pectin lyase.

BACKGROUND: Production of heterologous proteins in the E. coli periplasm, or into the extracellular fluid has many advantages; therefore naturally occurring signal peptides are selected for proteins translocation. The aim of this study was the production in high yields of a recombinant pectin lyase that is efficiently secreted and the encapsulation of transformed E. coli cells for pectin degradation in a biotechnological process. RESULTS: The nucleotide sequence of Bacillus subtilis alpha-amylase's signal peptide was fused to the N-terminal of an heterologously expressed pectin lyase in E. coli BL21 [DE3]. Thus pectin lyase secretion was achieved into the extracellular growth medium. E. coli cells harboring the recombinant plasmid heterologously express pectin lyase to around 22% of the total cellular proteins, as it was estimated by SDS-PAGE and image analysis. IPTG induces the heterologously expressed enzyme, which is initially distributed extracellularly (7 hour) and later on at the periplasmic (9 hours) or cytosolic fraction (20 hours). No pectin lyase activity was found in the membranes fraction and in the inclusion bodies. Encapsulation of the recombinant strains of E. coli in alginate or alginate/silica beads 1:5 showed that pectin lyase could degrade effectively its substrate, for at least ten operational cycles. CONCLUSION: Secretion of an heterologously overexpressed pectin lyase in E. coli BL21 [DE3] was achieved in this study. For this purpose the signal peptide of alpha-amylase from B. subtilis was fused to the N-terminal domain of pectin lyase. Encapsulated E. coli BL21 [DE3] cells harboring pET29c/exPNL were used successfully for pectin degradation up to ten operational cycles indicating that under special conditions this might have biotechnological implementations.

Journal Article↗

The hypocholesterolemic effect of lemon peels, lemon pectin, and the waste stream material of lemon peels in hybrid F1B hamsters.

BACKGROUND: We found in preliminary studies with hamsters that citrus peels have a cholesterol lowering effect comparable to that of pectin extracted from these peels. AIM OF THE STUDY: We wanted to examine whether the cholesterol lowering effect of the peels could be completely accounted for by the pectin in the peels. METHODS: We fed cholesterol enriched (0.1 %,w/w) semipurified diets containing 3% (w/w) of cellulose, lemon peels, lemon pectin, and the waste stream material of the lemon peels to hybrid F1B hamsters for a period of 8 weeks. The waste stream of the lemon peels is the left over after extraction of the lemon pectin. RESULTS: Feeding the semipurified diets resulted in an increase of plasma cholesterol levels in all the dietary groups after 2 and 4 weeks on the diets. Cholesterol concentrations in the cellulose fed hamsters continued to increase after 4 weeks on the diet, whereas cholesterol levels in the other groups had reached a plateau. As a consequence, the plasma cholesterol levels in the hamsters fed the peels (5.59 +/- 0.74 mmol/L, mean +/- SD, n = 14), pectin (5.19 +/- 0.48 mmol/L), or waste stream (5.53 +/- 0.94 mmol/L) were lower than those in the hamsters fed cellulose (6.71 +/- 1.52 mmol/L) after 8 weeks on the diets. Differences in total plasma cholesterol were reflected in differences in both VLDL and LDL cholesterol concentration, but this effect was more distinct for the VLDL. There was no effect of the type of fiber on HDL cholesterol levels. Liver cholesterol concentrations paralleled. the concentrations of plasma cholesterol and the liver cholesterol concentrations in the hamsters fed the peels (3.57+/- 1.01 micromol/g liver, mean +/- SD, n = 14), pectin (4.86 +/- 1.42), and the waste stream (4.96 +/- 1.89) were lower than those in the cellulose group (7.19 +/- 2.32). The hamsters fed the peels, pectin, or waste stream tended to have a higher excretion of fecal bile acids and neutral sterols then the cellulose fed hamsters. CONCLUSION: The results of this study suggest that lemon peels and the waste stream of the lemon peels are as effective in lowering plasma and liver cholesterol in hamsters as the pectin extracted from the peels and that also compounds other than pectin are probably responsible for the cholesterol lowering effect of the citrus peels.

Analysis of Variance↗

Characterization of pectin methyltransferase from soybean hypocotyls.

Pectin methyltransferase (PMT) catalyzing the transfer of the methyl group from S-adenosyl-L-methionine (SAM) to the C-6 carboxyl group of galactosyluronic acid residues in pectin was found in a membrane preparation of etiolated hypocotyls from 6-d-old soybean (Glycine max Merr.). The enzyme was maximally active at pH 6.8 and 35-40 degrees C, and required 0.5% (w/v) Triton X-100. The incorporation of the methyl group was significantly enhanced by addition of a pectin with a low (22%) degree of methyl-esterification (DE) as exogenous acceptor substrate. The apparent Michaelis constants for SAM and the pectin (DE22) were 0.23 mM and 66 microg x ml(-1), respectively. Attachment of the methyl group to the carboxyl group of the pectin via ester linkage was confirmed by analyzing radiolabeled product from incubation of the enzyme with [14C]methyl SAM and the acceptor pectin. Size-exclusion chromatography showed that both enzymatic hydrolysis with a pectin methylesterase and a mild alkali treatment (saponification) led to the release of radioactive methanol from the product. Enzymatic hydrolysis of the product with an endopolygalacturonase degraded it into small pectic fragments with low relative molecular mass, which also supports the idea that the methyl group is incorporated into the pectin. The soybean hypocotyls were fractionated into their cell wall components by successive extraction with water, EDTA, and alkali treatment. Among the resulting polysaccharide fractions, high PMT activity was observed when a de-esterified polysaccharide derived from the EDTA-soluble fraction (the pectic fraction) was added as an alternative acceptor substrate, indicating that the enzyme may be responsible for producing methyl-esterified pectin in vivo.

Cell Wall↗

Pectins: structure, biosynthesis, and oligogalacturonide-related signaling.

Pectin is a family of complex polysaccharides present in all plant primary cell walls. The complicated structure of the pectic polysaccharides, and the retention by plants of the large number of genes required to synthesize pectin, suggests that pectins have multiple functions in plant growth and development. In this review we summarize the current level of understanding of pectin primary and tertiary structure, and describe new methods that may be useful to study localized pectin structure in the plant cell wall. We also discuss progress in our understanding of how pectin is biosynthesized and review the biological activities and possible modes of action of pectic oligosaccharides referred to as oligogalacturonides. We present our view of critical questions regarding pectin structure, biosynthesis, and function that need to be addressed in the coming decade. As the plant community works towards understanding the functions of the tens of thousands of genes expressed by plants, a large number of those genes are likely to be involved in the synthesis, turnover, biological activity, and restructuring of pectin. A combination of genetic, molecular, biochemical and chemical approaches will be necessary to fully understand the function and biosynthesis of pectin.

Carbohydrate Conformation↗

Pectin-based systems for colon-specific drug delivery via oral route.

Pectin-derived matrices are now being examined and tested for controlled drug delivery. Pectin is intact in the upper gastrointestinal tract and degraded by colonic microflora. The composition of this microflora remains relatively consistent across a diverse human population. Thus, pectin-derived drug carriers provide promising potential for colon-specific drug delivery. This paper reviews recent developments in pectin-derived formulations. Subjects reviewed include gelation of pectin, calcium cross-linked pectinate, composites of pectin and other polymers, technologies to fabricate pectin into useful drug delivery vehicles, and methods to evaluate release kinetics of incorporated drugs. This article discusses advantages, limitations, and possible future developments in pectin-based formulations with particular emphasis on the field of colon-specific drug delivery.

Administration, Oral↗

DNA adducts in tissues of germ-free and conventional rats fed high- and low-esterified pectins.

Tissue samples from germ-free and conventional rats fed pectins with different degrees of esterification (DE) were tested for containing indigenous DNA adducts (I-compounds). For 21 days groups of six germ-free and 10 conventional rats each were fed either pectin-free or with diets containing 7.5% of three differently esterified pectin preparations (Pectin A, DE 92.6%; Pectin B, DE 70.8%; Pectin C, DE 34.5%). DNA was isolated from colonic mucosa, liver, lung, kidney and analysed for DNA adducts by the 32P-postlabelling assay. The experiments showed a tendency to a higher number and intensity of DNA-adduct-like spots (1) in the colonic mucosa compared with liver, lung, and kidney, (2) in germ-free compared with conventional rats, (3) with pectin-free compared with pectin-containing diets, (4) under the low-esterified compared with the higher-esterified pectins.

Animals↗

Electrosorption of pectin onto casein micelles.

Pectin, a polysaccharide derived from plant cells of fruit, is commonly used as stabilizer in acidified milk drinks. To gain a better understanding of the way that pectin stabilizes these drinks, we studied the adsorption and layer thickness of pectin on casein micelles in skim milk dispersions. Dynamic light scattering was used to measure the layer thickness of adsorbed pectin onto casein micelles in situ during acidification. The results indicate that the adsorption of pectin onto casein micelles is multilayered and takes place at and below pH 5.0. Renneting, i.e., cleaving-off kappa-casein from the casein micelles, did not alter the adsorption pH. It did, however, show that pectin arrests the rennet-induced flocculation of casein micelles below pH 5.0. From the findings we concluded the attachment of pectin onto casein micelles is driven by electrosorption. Adsorption measurements confirmed the multilayered nature of the adsorption of pectin onto casein micelles. Both the adsorbed amount and the layer thickness increased with decreasing pH in the relevant range 3.5-5.0. The phase behavior of a casein micelles/pectin mixture was determined and could be explained in terms of thermodynamic incompatibility being relevant above pH 5.0 and adsorption, leading to either stabilization and bridging, being relevant below pH 5.0. The results confirm that electrosorption is the driving force for the adsorption of pectin onto casein micelles.

Adsorption↗

The influence of wheat bran and pectin on the distribution of water in rat caecal contents and faeces.

Wheat bran and pectin (100 g/kg) were added to a basal diet and fed to rats. An in vitro dialysis technique was used to measure the distribution of caecal and faecal water between the bound, i.e. that held by bacteria and undigested macromolecules, and free water. Bran increased wet (67%) and dry (74%) faecal weight. Pectin increased wet faecal weight (59%), but did not influence dry weight. In faeces both bran and pectin increased the amount of total and bound water, but only pectin increased total and bound water when expressed on a dry weight basis. Caecal wet (90%) and dry (67%) weights increased with pectin but not with bran. Bran did not change total water but increased bound water whereas pectin increased both. This suggests that water contributed more to the increase in stool bulk in the pectin-supplemented animals due to free and bound water associated with both increased numbers of bacteria and residual pectin. Pectin altered the distribution of water in faeces. Bran has no effect on water distribution and is only partly fermented. The residual water-holding capacity leads to an increased wet and dry stool output.

Animals↗

Release characteristics of pectin microspheres prepared by an emulsification technique.

The potential application of pectin as a matrix polymer for making microspheres by an emulsification technique was explored, and the drug release property of these pectinate microspheres containing drug cores of varying aqueous solubilities: sulphanilamide, sulphaguanidine and sulphathiazole, was investigated using different dissolution media. The size and size distribution, specific surface area, drug content and drug release property of the pectinate microspheres were determined. The solubility and solution pH of drugs and their propensity to interact with pectin were characterized. Pectinate microspheres were successfully prepared by external gelation, using a modified emulsification technique. The kinetics of drug release from the microspheres best fitted Higuchi's model. Interestingly, the lowest percentage of drug released was produced by microspheres which were smallest in size and, therefore, largest in specific surface area, and containing sulphanilamide, the most aqueous soluble and the lowest molecular weight drug. Mathematical correlation study indicated that the drug release profile of pectinate microspheres was notably affected by the drug content and the extent of drug-pectin interaction in the microspheres. Generally, a higher percentage of drug was released from the microspheres with a higher drug content and/or lower extent of drug-pectin interaction. The extent of drug-pectin interaction was highest in microspheres containing sulphanilamide, followed by sulphaguanidine and sulphathiazole, opposite to that of drug content.

Delayed-Action Preparations↗

Alginate-pectin microcapsules as a potential for folic acid delivery in foods.

Most naturally occurring folate derivatives in foods are highly sensitive to temperature, oxygen, light and their stability is affected by processing conditions. Folic acid incorporated microcapsules using alginate and combinations of alginate and pectin polymers were prepared to improve stability. Folic acid stability was evaluated with reference to encapsulation efficiency, gelling and hardening of capsules, capsular retention during drying and storage. Use of alginate in combination with pectin produced more robust capsules and contributed to greater encapsulation efficiency. The capsules lost their spherical shape as a consequence of increased pectin. The high alginate capsules, A100:P0 (100% alginate: 0% pectin) and A80:P20 (80% alginate: 20% pectin) were of regular spherical shape, while those with more pectin, A70:P30 (70% alginate: 30% pectin) and A60:P40 (60% alginate: 40% pectin) formed irregular spheres. The loading efficiency, expressed as a percentage of the actual loading to theoretical loading, varied from 55-89% with the composition of the mixed polymers. After 11 weeks of storage at 4 degrees C, folic acid retention in freeze-dried capsules was 100% (A70:P30 and A60:P40), 80% (A80:P20) and 30% (A100:P0). The blended alginate and pectin polymer matrix increased folic acid encapsulation efficiency and reduced the leakage from the capsules compared to those made with alginate alone and showed higher folic acid retention after freeze drying and storage.

Alginates↗