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1.
《Cereal Chemistry》2017,94(6):922-927
The degradation of inositol hexakisphosphate (IP6) was evaluated in whole meal wheat dough fermented with baker's yeast without phytase activity, different strains of Saccharomyces cerevisiae (L1.12 or L6.06), or Pichia kudriavzevii with extracellular phytase activity to see if the degradation of IP6 in whole meal dough and the corresponding bread could be increased by fermentation with phytase‐active yeasts. The IP6 degradation was measured after the dough was mixed for 19 min, after the completion of fermentation, and in bread after baking. Around 60–70% of the initial value of IP6 in the flour (10.02 mg/g) was reduced in the dough already after mixing, and additionally 10–20% was reduced after fermentation. The highest degradation of IP6 was seen in dough fermented with the phytase‐active yeast strains S. cerevisiae L1.12 and P. kudriavzevii L3.04. Activity of wheat phytase in whole meal wheat dough seems to be the primary source of phytate degradation, and the degradation is considerably higher in this study with a mixing time of 19 min compared with earlier studies. The additional degradation of IP6 by phytase‐active yeasts was not related to their extracellular phytase activities, suggesting that phytases from the yeasts are inhibited differently. Therefore, the highest degradation of IP6 and expected highest mineral bioavailability in whole meal wheat bread can be achieved by use of a phytase‐active yeast strain with less inhibition. The strain S. cerevisiae L1.12 is suitable for this because it was the most effective yeast strain in reducing the amount of IP6 in dough during a short fermentation time.  相似文献   

2.
Lactic acid fermentation of cereal flours resulted in a 100 (rye), 95-100 (wheat), and 39-47% (oat) reduction in phytate content within 24 h. The extent of phytate degradation was shown to be independent from the lactic acid bacteria strain used for fermentation. However, phytate degradation during cereal dough fermentation was positively correlated with endogenous plant phytase activity (rye, 6750 mU g(-1); wheat, 2930 mU g(-1); and oat, 23 mU g(-1)), and heat inactivation of the endogenous cereal phytases prior to lactic acid fermentation resulted in a complete loss of phytate degradation. Phytate degradation was restored after addition of a purified phytase to the liquid dough. Incubation of the cereal flours in buffered solutions resulted in a pH-dependent phytate degradation. The optimum of phytate degradation was shown to be around pH 5.5. Studies on phytase production of 50 lactic acid bacteria strains, previously isolated from sourdoughs, did not result in a significant production of intra- as well as extracellular phytase activity. Therefore, lactic acid bacteria do not participate directly in phytate degradation but provide favorable conditions for the endogenous cereal phytase activity by lowering the pH value.  相似文献   

3.
Activities of phytase, a pH 6.0 optimum nonspecific phosphomonoesterase and phosphodiesterase assayed toward bis(p-nitrophenyl)phosphate (phosphodiesterase I) and against p-nitrophenylphosphorylcholine (phosphodiesterase II), were partially purified from mycelial extracts of Aspergillus niger AbZ4 cultivated on a molasses medium by a liquid surface fermentation method. After elimination of phosphate from the medium, 7.3- and 3.5-fold enhancements in specific activities of phytase and phosphodiesterase II were observed. Efficacies of mycelial protein fractions in dephosphorylating a wheat-based broiler feed were determined in vitro according to a procedure that simulated digestion in the intestinal tract of poultry. The addition of 0.052 mg of protein from fractions, each of which was high in either pH 6.0 optimum phosphomonoesterase, phosphodiesterase I, phosphodiesterase II, or phytase per gram of a feed sample resulted in the enhancement of phosphorus release by 10, 11, 27, and 88%, respectively. In the presence of an excess of commercial phytase, the addition of the mycelial fraction high in phytase increased the dephosphorylation rate by 56%. The fraction high in phosphodiesterase II enhanced feed dephosphorylation by 8% in the presence of an excess of commercial phytase and commercial acid phosphatase.  相似文献   

4.
In this study, the influence of phytase-producing Bifidobacterium strains during the breadmaking process (direct or indirect) on final bread Fe dialyzability and ferritin formation in Caco-2 cell as a measure of cell Fe uptake was assessed. The addition of bifidobacteria significantly reduced the InsP(6) + InsP(5) concentrations compared to control samples. Fe-dialyzable contents for samples with bifidobacteria were increased 2.3-5.6-fold, and dialyzability was improved by 2.6-8.6% compared to controls. However, this was not reflected in an increase of Fe uptake by Caco-2 cells as was predicted by the phytate/Fe molar ratios. The results demonstrated the usefulness of phytase-producing bifidobacteria to reduce phytate during the breadmaking process and to increase Fe accessibility, although the effects appeared to be still insufficient to improve Fe bioavailability in Caco-2 cells. Further refinement of the use of phytase-producing bifidobacterial strains and/or breadmaking technological processes is deserved for improving Fe uptake.  相似文献   

5.
A phytate-degrading enzyme was purified approximately 2190-fold from germinated 4-day-old faba bean seedlings to apparent homogeneity with a recovery of 6% referred to the phytase activity in the crude extract. It behaves as a monomeric protein of a molecular mass of approximately 65 kDa. The phytate-degrading enzyme belongs to the acidic phytases. It exhibits a single pH optimum at 5.0. Optimal temperature for the degradation of sodium phytate is 50 degrees C. Kinetic parameters for the hydrolysis of sodium phytate are K(M) = 148 micromol L(-1) and k(cat) = 704 s(-1) at 35 degrees C and pH 5.0. The faba bean phytase exhibits a broad affinity for various phosphorylated compounds and hydrolyzes phytate in a stepwise manner. The first hydrolysis product was identified as D/L-myo-inositol(1,2,3,4,5)pentakisphosphate.  相似文献   

6.
Phytases hydrolyze myo-inositol 1,2,3,4,5,6-hexaphosphate (IP(6)), yielding lower inositol phosphates and inorganic orthophosphate. Two commercial strains of baker's yeast (Saccharomyces cerevisiae), Y(1) and Y(2), were able to express phytase activity. This was determined by the capacity to grow in a synthetic medium with IP(6) as the sole phosphorus source. IP(6) hydrolysis was rapid for both strains, and after 24 h, all IP(6) was degraded. Control cultures contained inorganic orthophosphate (P(i)) and no IP(6). Growth rate in IP(6) medium was for both strains essentially identical to growth in P(i) medium, indicating a well-adapted metabolism for utilization of phosphorus from IP(6). There was some difference in growth yield (milligrams of biomass per milligram of glucose) between the two strains: 0.95 (Y(1)) and 1.35 (Y(2)) in IP(6) medium and 1.03 and 1. 35, respectively, in P(i) medium. The phytases were of the 3-phytase type, forming mainly DL-Ins(1,2,4,5,6)P(5), DL-Ins(1,2,5,6)P(4), and DL-Ins(1,2,6)P(3).  相似文献   

7.
Using a multivariate experimental design, optimal conditions for phytate degradation were found to be pH 4.8 and 57 degrees C in barley flour (cv. Blenheim) and pH 5.2 and 47 degrees C in a crude extracted phytase from barley. Three methods for measuring phytase activity in raw and hydrothermally processed barley were compared. Incubation at pH 5 and 55 degrees C for 60 min did not give significantly different results (p > 0.05), whereas incubation at pH 5 and 50 degrees C for 10, 20, 30, and 60 min gave significantly different results (p < 0.001) between methods. The change in microstructure of phytate globoids during hydrothermal processing showed that the degradation was highest in the scutellum cells and less in the aleurone layer.  相似文献   

8.
During food processing such as baking, phytate is dephosphorylated to produce degradation products, such as myo-inositol pentakis-, tetrakis-, tris-, bis-, and monophosphates. Certain myo-inositol phosphates have been proposed to have positive effects on human health. The position of the phosphate groups on the myo-inositol ring is thereby of great significance for their physiological functions. Using a combination of high-performance ion chromatography analysis and kinetic studies the stereospecificity of myo-inositol hexakisphosphate dephosphorylation by a phytate-degrading enzyme from baker's yeast (Saccharomyces cerevisiae) was established. The data demonstrate that the phytate-degrading enzyme from baker's yeast dephosphorylates myo-inositol hexakisphosphate in a stereospecific way by sequential removal of phosphate groups via D-Ins(1,2,4,5,6)P(5), D-Ins(1,2,5,6)P(4), D-Ins(1,2,6)P(3), D-Ins(1,2)P(2), to finally Ins(2)P (notation 3/4/5/6/1). Knowledge of the absolute stereochemical specificity of the baker's yeast phytase allows use of the enzyme to produce defined myo-inositol phosphates for kinetic and physiological studies.  相似文献   

9.
The effect of the soil environment on the mobility, stability and catalytic activity of phytase from two sources was compared, as these factors have important implications for the efficacy of enzyme function in soil. Phytase from an ascomycete fungus (Aspergillus niger) and a basidiomycete fungus (Peniophora lycii) was added to soil suspensions from three contrasting soils and activities in the solution and solid phase were monitored. The two enzymes were compared because the P. lycii phytase was known to have greater specific activity and a more acidic isoelectric point (pI) than A. niger and therefore predicted to have different adsorption characteristics. When added to soil suspensions buffered at pH 7.5, both phytases remained in solution in all of the soils. In contrast at near natural soil pH (pH 5.5), only the P. lycii phytase remained in solution, while the A. niger phytase was rapidly adsorbed to the soil solid phase. The extent of this adsorption was reduced, however, in a soil-dependent manner by prior addition of bovine serum albumin (BSA) to the soil suspensions. At the natural pH of the soil, the stability of the P. lycii phytase in soil solution was improved under sterile conditions, whereas degradation of the A. niger phytase was unaffected. Subsequently, P. lycii phytase was shown to be more effective at hydrolysing myo-inositol hexakisphosphate added to the soil. Moreover, the P. lycii phytase also hydrolysed more organic phosphate that was endogenous to a range of soils. This research indicates that the physicochemical properties of fungal phytases affect their mobility and temporal stability and their capacity to hydrolyse inositol phosphates in soil environments.  相似文献   

10.
Phytase is used commercially to maximize phytic acid degradation and to decrease phosphorus levels in poultry and swine manure. To determine phytase content in edible mushrooms, basidiomata of Agaricus bisporus and three specialty mushrooms (Grifola frondosa, Lentinula edodes, and Pleurotus cornucopiae) and spent mushroom substrate (SMS) were surveyed. Enzyme activity ranged from 0.046 to 0.074 unit/g of tissue for four A. bisporus types (closed and open whites and closed and open browns) grown at The Pennsylvania State University's Mushroom Test Demonstration Facility (MTDF). The addition of various nutrient supplements to phase II mushroom production substrate did not alter phytase activity in A. bisporus. Portabella mushrooms (open brown) obtained from a commercial farm had significantly higher levels of phytase activity (0.211 unit/g of tissue) compared to A. bisporus grown at the MTDF. Of the specialty mushrooms surveyed, maitake (G. frondosa) had 20% higher phytase activity (0.287 unit/g of tissue) than commercial portabella mushrooms. The yellow oyster mushroom (P. cornucopiae) ranked second in level of phytase activity (0.213 unit/g of tissue). Shiitake (L. edodes) contained the least amount of phytase in basidiomata (0.107 unit/g of tissue). Post-crop steam treatment (60 degrees C, 24 h) of SMS reduced phytase activity from 0.074 to 0.018 unit/g. Phytase was partially purified from commercially grown portabella basidiomata 314-fold with an estimated molecular mass of 531 kDa by gel filtration chromatography. The optimum pH for activity was 5.5, but appreciable phytase activity was observed over the range of pH 5.0-8.0. Partially purified A. bisporus phytase was inactivated following a 10-min incubation at > or =60 degrees C.  相似文献   

11.
The fungal PhyA protein, which was first identified as an acid optimum phosphomonoesterase (EC 3.1.3.8), could also serve as a vanadate haloperoxidase (EC 1.11.1.10) provided the acid phosphatase activity is shut down by vanadate. To understand how vanadate inhibits both phytate and pNPP degrading activities of fungal PhyA phytase and bacterial AppA2 phytase, kinetic experiments were performed in the presence and absence of orthovanadate and metavanadate under various acidic pHs. Orthovanadate was found to be a potent inhibitor at pH 2.5 to 3.0. A 50% activity of fungal phytase was inhibited at 0.56 μM by orthovanadate. However, metavanadate preferentially inhibited the bacterial AppA2 phytase (50% inhibition at 8 μM) over the fungal phytase (50% inhibition at 40 μM). While in bacterial phytase the K(m) was not affected by ortho- or metavanadate, the V(max) was reduced. In fungal phytase, both the K(m) and V(max) was lowered. The vanadate exists as an anion at pH 3.0 and possibly binds to the active center of phytases that has a cluster of positively charged Arg, Lys, and His residues below the enzymes' isoelectric point (pI). The active site fold of haloperoxidase was shown to be very similar to fungal phytase. The vanadate anions binding to cationic residues in the active site at acidic pH thus serve as a molecular switch to turn off phytase activity while turning on the haloperoxidase activity. The fungal PhyA phytase's active site housing two distinct reactive centers, one for phosphomonoesterase and the other for haloperoxidase, is a unique example of how one protein could catalyze two dissimilar reactions controlled by vanadate.  相似文献   

12.
The interaction between protein and phytate was investigated in vitro using proteins extracted from five common feedstuffs and from casein. The appearance of naturally present soluble protein-phytate complexes in the feedstuffs, the formation of complexes at different pHs, and the degradation of these complexes by pepsin and/or phytase were studied. Complexes of soluble proteins and phytate in the extracts appeared in small amounts only, with the possible exception of rice pollards. Most proteins dissolved almost completely at pH 2, but not after addition of phytate. Phytase prevented precipitation of protein with phytate. Pepsin could release protein from a precipitate, but the rate of release was increased by phytase. Protein was released faster from a protein-phytate complex when phytase was added, but phytase did not hydrolyze protein. Protein was released from the complex and degraded when both pepsin and phytase were added. It appears that protein-phytate complexes are mainly formed at low pH, as occurs in the stomach of animals. Phytase prevented the formation of the complexes and aided in dissolving them at a faster rate. This might positively affect protein digestibility in animals.  相似文献   

13.
Interactions with food components may alter the resistance of food proteins to digestion, a property thought to play an important role in determining allergenic properties. The kinetics of breakdown of the bovine milk allergen alpha-lactalbumin during in vitro gastrointestinal digestion was found to be altered by interactions with physiologically relevant levels of phosphatidylcholine (PC), a surfactant that is abundant both in milk and is actively secreted by the stomach. Breakdown during gastric digestion was slowed in the presence of PC and accompanied by small alterations in the profile of resulting peptides, with little effect being observed during subsequent duodenal digestion. alpha-Lactalbumin was found to unfold at gastric (acid) pH, giving a CD spectrum similar to that obtained for the partially folded state it is known to adopt at pH values below its isoelectric point. Fluorescence polarization studies performed at low pH indicated that this partially unfolded form of the protein was able to penetrate into the PC vesicles. These interactions are probably responsible for the slowing of gastric digestion by reducing the accessibility of the protein to pepsin. These findings show that interactions with other food components, such as lipids, may alter the rate of breakdown of food proteins in the gastrointestinal tract. It underlines the importance of the food matrix in affecting patterns of food allergen digestion and hence presentation to the immune system and that in vitro digestion systems used for assessing digestibility of allergens must take account of surfactants.  相似文献   

14.
Brook trout, Salvelinus fontinalis, embryos and fry from three sources (an acidic watershed in Kejimkujik Park at pH 4.7 to 5.3, a neutral watershed at pH 7, a hatchery at pH 7) were exposed separately to lethal and sublethal levels of acidity (pH 7.0, 5.2, 4.7, 4.3, 3.9), beginning at fertilization. Significant differences in mortality between the strains at low pH were observed and these suggested a genetic component to acid tolerance. Mortality in the strain from the acidic watershed was the lowest, followed by the second wild strain. Survival in both wild strains at low pH was much better than survival in hatchery embryos. These differences in survival at sublethal acidity (4.7 to 7.0) were principally the result of high mortality shortly after fertilization. After this period, survival stabilized. Only at pH 4.3 did substantial mortality occur at hatching. The early embryonic stage therefore appears to be the most susceptible to sublethal acid stress in brook trout. Hatchery strain embryos were also introduced at the eyed stage at 213 degree-days. Subsequent survival of this group was better at low pH than that of hatchery embryos introduced at fertilization, thereby indicating an early or cumulative deleterious effect. Higher acidity retarded hatch in all cases. The time to 50% hatch was delayed by 1.2 degree-days with each increase of 1 μM H+.  相似文献   

15.
Lactic acid bacteria were screened from feces of newborn baby and from dongchimi. Selection criteria employed included the ability of strains to withstand environmental conditions such as low pH, high bile concentration, and oxygen. The isolates were applied to the juice of various vegetables, and fermentabilities of isolates were compared. Strains F20-3, F35-3, and F35-6 showed high stability compared to the other strains at pH 3.0 and 2.3. Strains D1 and D2 showed the highest survival at pH 3.0 and survived at 1% high bile concentration. The selected strains were able to survive at low pH and relatively high bile concentration and were not affected by oxygen. The growth of isolates was >10(7) cfu/mL in natural media, and strains were not affected by the pH values of the vegetables. Therefore, isolated strains are thought to survive through the intestinal ecosystem and are considered to be suitable for application of the fermented product using various vegetables for their functionality. The isolates were identified as Lactobacillus plantarum and Lactobacillus fermentum.  相似文献   

16.
Phytate, inositol hexaphosphate (InsP(6)), may be hydrolyzed to inositol phosphates with lower degree of phosphorylation, i.e., inositol penta- to monophosphates (InsP(5)-InsP(1)), during food processing. Each of these lower inositol phosphates exists in different isomeric forms. The objective of this study was to determine if different isomers of InsP(3)-InsP(5) (Ins(1,2,4)P(3), Ins(1,2,3)P(3), Ins(1,2,6)P(3), Ins(1,3,4)P(3), Ins(1,2,3,4)P(4), Ins(1,2,5,6)P(4), Ins(1,2,4,5,6)P(5), and Ins(1,3,4,5,6)P(5)) and InsP(6) affect the uptake of iron. We studied the iron absorption in vitro using the human intestinal epithelial cell line, Caco-2. Addition of a 2-fold molar excess of InsP(6) or InsP(5) in proportion to Fe (1 h incubation at 37 degrees C) reduced iron uptake by 46-52% (p < 0.001). Neither InsP(4) isomers nor InsP(3) isomers affected iron uptake significantly at 1 h incubation with a molar InsP:Fe level of 2:1. Iron uptake was shown to not be a function of the isomeric form of inositol phosphates. The inositol phosphate isomers did not seem likely to interact with each other through iron to form more stable iron complexes. At a molar InsP:Fe level of 20:1 an inhibitory effect of InsP(4) was found, while InsP(3) did not affect the iron absorption even at a 20-fold molar excess.  相似文献   

17.
Broccoli (Brassica oleracea L. var. italica cv. Marathon) inflorescences are a good source of bioactive compounds, such as phenolics (flavonoids and hydroxycinnamoyl derivatives), glucosinolates, and vitamin C. In this work, these health-promoting compounds were submitted to digestion under in vitro gastrointestinal conditions (pH, temperature, enzyme, and chemical conditions). This technique differentiated among the compounds associated with macromolecules in soluble and insoluble form and those that are freely soluble. In addition, it evaluates the chemical stability of the broccoli compounds under simulated physiological conditions. The gastric digestion of broccoli caused high losses in glucosinolates (69% loss), whereas phenolics and vitamin C presented higher stability under these conditions. Thus, there were no losses in flavonoids, a 7% loss of vitamin C, and a variable rate of loss (6-25%) in hydroxycinnamic acid derivatives. The stability of all of the compounds was affected by the in vitro intestinal conditions. Under the in vitro conditions, flavonoids and hydroxycinnamoyl acid derivatives were of low availability, due to their significant losses under these conditions, at the end of the experiment (84 and 80% loss, respectively). Vitamin C was the metabolite that showed the greater decrease after intestinal digestion (91% loss). Regarding the remaining glucosinolates, these compounds presented higher stability under intestinal conditions, rendering an availability similar to that found for phenolics (75% loss). Therefore, broccoli components were affected by gastric and/or intestinal conditions depending on the type of compound. Thus, glucosinolates were mainly degraded by gastric conditions, whereas phenolic compounds and vitamin C were degraded by intestinal conditions.  相似文献   

18.
Wheat phytase was purified to investigate the action of the enzyme toward its pure substrate (phytic acid - myo-inositol hexakisphosphate) and its naturally occurring substrate (phytate globoids). Phytate globoids were purified to homogeneity from wheat bran, and their nutritionally relevant parameters were quantified by ICP-MS. The main components of the globoids were phytic acid (40% w/w), protein (46% w/w), and several minerals, in particular, K > Mg > Ca > Fe (in concentration order). Investigation of enzyme kinetics revealed that K(m) and V(max) decreased by 29 and 37%, respectively, when pure phytic acid was replaced with phytate globoids as substrate. Time course degradation of phytic acid or phytate globoids using purified wheat phytase was followed by HPIC identification of inositol phosphates appearing and disappearing as products. In both cases, enzymatic degradation initiated at both the 3- and 6-positions of phytic acid and end products were inositol and phosphate.  相似文献   

19.
多环芳烃高效降解菌的筛选   总被引：1，自引：1，他引：1  
以多环芳烃(PAHs)菲、蒽、芘、■和苯并(a)芘为供试物,对土著混合菌和引进菌同时进行筛选实验。结果表明,引进菌和土著混合菌经过驯化后对菲、蒽、芘、■和苯并(a)芘均具有一定的降解能力。其中,在pH=6时,混合菌U03在48h内对5种PAHs的降解率均相对较高,分别为:72.38%;64.46%;65.77%;66.49%和64.77%,并且其的降解速率在各菌剂中同样最快,通过SPSS数理统计分析软件对数据进行处理后得出,混合菌U03可在较短时间内达到较好的降解目的。室内模拟试验证明混合菌U03具有较强的降解PAHs的能力,混合菌的协同作用有利于污染土壤中PAHs的降解。  相似文献   

20.
myo-Inositol hexaphosphate (IP6) is the main source of phosphorus in cereal grains, and therefore, in bakery products. Different microorganisms such as yeasts and lactic acid bacteria have phytase enzymes able to hydrolyze IP6 during the wholemeal breadmaking. In this paper, the phytase activity of Lactobacillus plantarum, Lactobacillus brevis, Lactobacillus curvatus, and Saccharomyces cerevisiae strains, isolated from southern Italian sourdoughs, is assayed using the (31)P NMR technique. The sourdough technology based on the use of lactic acid bacteria in the breadmaking is finally suggested.  相似文献   

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