Prolamin Fractions Research Articles

Chemical Profiles and Antioxidant Activities of Leaf, Pulp, and Stone of Cultivated and Wild Olive Trees (Olea Europaea L.)

ABSTRACT In this study, the phytochemical profile including the fatty acids composition and the minerals, the polyphenols, and the proteins contents were quantified on leaves, pulp, and stone of two oleasters trees from southern Tunisia. Two olive cultivars (Zarrazi and Chemlali) were used for comparisons. The antioxidant activities were conducted using the 2,2′-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) and the 2,2-diphenylpicrylhydrazyl (DPPH) assays. Results showed that the pulp and the stone of oleasters (wild olives) were richer in total lipid having, respectively, 16.30% and 9.42% of Dry Weight basis (DW). Qualitatively, the fatty acids profile of pulp and stone from cultivars and oleasters was identical. The oleic acid is the major fatty acid having the highest percentage in the oils from the stone of oleaster1 (69.08%) followed by linoleic acid. However, quantitatively, significant differences in fatty acids composition were noted. The oleaster stones were richer in storage proteins showing that the globulin is the major fraction (50.47%), followed by albumin (25.72%), prolamin (17.61%), and glutelin (6.19%) fractions. Concerning the minerals, results showed that the pulp is richer in potassium (862.87 mg/100 g DW) than leaves (526.50 mg/100 g DW) and stone (136.50 mg/100 g DW). In contrast, the leaves have the highest phosphorus content (42.74 mg/100 g DW). The highest polyphenols content was 711.55 mg/100 g DW in the pulp followed by the leaves and stone. The leaves, pulp, and stone extracts showed high antioxidant activities using DPPH and ABTS assays. The oleasters seem to be a potential source of edible oil, protein, and antioxidants. They could be used as supplements and/or ingredients in oil and fat industries.

Speciation of Selenium in Brown Rice Fertilized with Selenite and Effects of Selenium Fertilization on Rice Proteins.

Foliar Selenium (Se) fertilizer has been widely used to accumulate Se in rice to a level that meets the adequate intake level. The Se content in brown rice (Oryza sativa L.) was increased in a dose-dependent manner by the foliar application of sodium selenite as a fertilizer at concentrations of 25, 50, 75, and 100 g Se/ha. Selenite was mainly transformed to organic Se, that is, selenomethionine in rice. Beyond the metabolic capacity of Se in rice, inorganic Se also appeared. In addition, four extractable protein fractions in brown rice were analyzed for Se concentration. The Se concentrations in the glutelin and albumin fractions saturated with increasing Se concentration in the fertilizer compared with those in the globulin and prolamin fractions. The structural analyses by fluorescence spectroscopy, Fourier transform infrared spectrometry, and differential scanning calorimetry suggest that the secondary structure and thermostability of glutelin were altered by the Se treatments. These alterations could be due to the replacements of cysteine and methionine to selenocysteine and selenomethionine, respectively. These findings indicate that foliar fertilization of Se was effective in not only transforming inorganic Se to low-molecular-weight selenometabolites such as selenoamino acids, but also incorporating Se into general rice proteins, such as albumin, globulin glutelin, and prolamin, as selenocysteine and selenomethionine in place of cysteine and methionine, respectively.

The effects of protein-phenolic interactions in wheat protein fractions on allergenicity, antioxidant activity and the inhibitory activity of angiotensin I-converting enzyme (ACE)

Abstract Protein fractions were isolated from wheat flour including albumin, globulin, glutelin-1, glutelin-2 and prolamin. The free and bound phenolics were extracted from each protein fraction to determine the impact of their removal on allergenicity, antioxidant activity and the inhibitory activities of the angiotensin converting enzyme. The glutelin-1 fraction showed the highest protein content and yield of 71.02% and 21.02%, respectively. The highest antioxidant activity was noted in the glutelin-1 fraction (48.17%). The angiotensin converting enzyme inhibitory activities among the protein fractions ranged from 6.87% to 84.52%. The greatest reduction of allergenicity (39.66%) was demonstrated in the prolamin fraction. We conclude that the removal of phenolics appears to decrease significantly the allergenicity of wheat protein fractions while maintaining significant bioactivities related to anti-hypertensive, antioxidant, and anti-diabetic properties.

Isolation and characterisation of antioxidative peptides from bromelain-hydrolysed brown rice protein by proteomic technique.

In this study, proteins from Thai brown rice (Khao Dawk Mali 105) were separated into albumin (2.18 %), globulin (3.98 %), glutelin (84.23 %), and prolamin (9.61 %) fractions, and were hydrolysed with various bromelain concentrations and hydrolysis times. Liquid chromatography-electrospray ionization/mass spectrometry (LC-ESI-MS/MS) was conducted to assess the composition, molecular weight (MW) distribution, and sequence of the resulting peptides, and showed that most peptides have a MW below 2000 Da (60-70 %). Glutelin fraction hydrolysates exhibited the highest 2,2'-azino-bis 3-ethylbenzthiazoline-6-sulfonic (ABTS•+) radical-scavenging (0.69 ± 0.04 µM trolox) and copper chelating (4.12 ± 0.01 mg ethylenediaminetetraacetic acid; EDTA) activities, which was further fractionated into six fractions using reversed-phase high-performance liquid chromatography. The fourth fraction showed the highest ABTS•+ scavenging (1.08 ± 0.03 mM trolox) and copper chelating (5.00 ± 0.02 mg EDTA) activity. LC-MS/MS analysis revealed that the peptides with MW less than 1500 Da and hydrophobic or aromatic N-terminal residues, such as SPFWNINAHS, MPVDVIANAYR, VVYFDQTQAQA, and VEVGGGARAP, possibly contributed to the highest antioxidant activity in fourth fraction.

Biuret and Bradford Methods Suitability for Protein Quantification in Rapeseed Meal

Summary Being attractive for insects, non-genetically modified rapeseed is valuable for maintaining environmental biodiversity. Primarily, the rapeseed is an important industrial crop which is used for production of vegetable oil. Oil extraction from rapeseeds results in the generation of substantial amounts of rapeseed meal which is used either as a protein rich feed additive or as a source for preparation of protein containing ingredients for food industry. Both applications require frequent evaluation of protein content. Although Kjeldahl method is considered standard, it is not appropriate for routine evaluation of protein content in protein extracts. The aim of the study was to evaluate suitability of biuret and Bradford methods for protein quantification in rapeseed meal extracts. After consecutive triple extraction of proteins with water, 5% NaCl, 70% ethyl alcohol and 0.1 N NaOH, protein evaluation of each albumin, globulin, prolamin and glutelin extraction aliquot demonstrated overall lower protein content by Bradford method compared to biuret method. The most pronounced differences in protein content were observed with prolamin fraction where three fold higher protein concentrations in each extraction aliquot was observed when biuret method was applied for the evaluation. Comparative quantification of the total protein of each of the four fractions followed a similar trend of lower protein content evaluation by Bradford method. Overall results indicated biuret method as more suitable for protein quantification in rapeseed meal extracts which was confirmed by comparison with data obtained by Kjeldahl method.

An Effective Gluten Extraction Method Exploiting Pure Choline Chloride-Based Deep Eutectic Solvents (ChCl-DESs)

Gluten analysis is still affected by the lack of an efficient and universal extraction solvent for gliadin, i.e., the prolamine fraction of gluten which is the analytical target used to quantify gluten in food. In this investigation, the possibility of adopting pure choline chloride deep eutectic solvents (ChCl-DESs) as gliadin extraction media was tested. As prototypes of ChCl-DESs, ethaline and reline were chosen in view of their good dipolar and hydrogen bond donor (HBD) properties, as well as of their moderate enough viscosity. Their ability to act as effective solvents for gliadin and their inability to affect the subsequent gliadin detection by a frequently adopted and commercially available ELISA kit were first assessed. Ethaline and reline extraction performance was then tested by evaluating gliadin recoveries achieved on gluten-free food real samples before and after their spiking with controlled gliadin amounts. Higher recoveries were found by using these DESs in comparison with those gained by the usually adopted 60% (v/v) ethanol-water solvent. In fact, gluten recoveries ranging from 78 to 113%, with a RSD better than 13%, were achieved by using ethaline. Less good recoveries (from 67 to 132% with a RSD of 20%) were achieved with reline, even though they were however better than those found with 60% v/v ethanol-water solvent. These results make the proposed media profitable solvents for gliadin extraction and its subsequent detection by a commonly used immunoassay kit, without any change of the usual detection procedure.

Molecular characterization and bio-functional property determination using SDS-PAGE and RP-HPLC of protein fractions from two Nigella species.

This study aimed to investigate the molecular and bio-functional properties of protein fractions from Nigella damascena and Nigella arvensis, including the albumin, globulin, glutein-1, glutein-2 and prolamin fractions. Protein subunits were not observed in globulin and prolamin fractions. No peaks appeared in RP-HPLC chromatograms of globulin for either species. Two predominant peaks were observed in the RP-HPLC profiles of all protein fractions. Proteins separated by RP-HPLC have potential inhibitory and antioxidant activities in all fractions. Optimum ACE-inhibitory and antioxidant activities of proteins separated by RP-HPLC were observed in glutein-2 and albumin, respectively, for both species. For pepsin and combined pepsin-trypsin hydrolyses, the highest degree of hydrolysis (DH) was obtained in glutein-2 fraction of Nigella arvensis. Highest ACE-inhibitory activity of hydrolyzed protein fractions was found at 4h via pepsin hydrolysis in globulin fraction of Nigella damascena. Highest antioxidant activities of hydrolyzed protein fractions were found in glutelin-2 for both species.

Non-prolamin fraction from brewer’s spent grain: a novel plant-based emulsifier

Brewer’s spent grain (BSG) is a major by-product generated in brewing process, but has received little attention and needs to be subjected to value addition. The present study is aimed at fractionation of non-prolamin and prolamin proteins from wheat beer BSG, and to explore their emulsification potential. Preliminary studies showed emulsions made using non-prolamin fraction of BSG were stable, while there was a rapid fall observed in emulsion stability for prolamin fraction as measured at 30–150 min. Further studies using non-prolamin fraction showed emulsification activity index and emulsion stability of 245.6 m2 g−1 and 9.8% at pH 4, which increased with a rise in pH to 560 m2 g−1 and 90% at pH 9 respectively. Polyacrylamide gel electrophoresis (PAGE) of the non-prolamin fraction revealed a distinct band between 40–205 kD attributed to globulins, and bands with molecular weight <30 kD from albumins of wheat and barley. On estimation of zeta-potential it was seen that minimum surface charge was obtained at more than one pH value. Multiple pI values between 4 and 4.2 and 4–6.7 highlight the presence of multiple proteins and subunits as affirmed from PAGE. The obtained results enabled fractionation of non-prolamin and prolamin fractions of wheat beer BSG. The non-prolamin protein fraction isolated from beer industry waste could serve as a novel plant-based emulsifier with high value application in food industry.

Protein fractionation and its Invitro hemagglutinating activity of Star anise extracts

Star anise ( Illicium verum ) is an aromatic evergreen tree bearing purple-red flowers and anise-scented star-shaped fruit. It carry chemical compounds known to have antioxidant, disease preventing and health promoting properties. It's application is in many traditional medicines such as antispasmodic, digestive stimulant and toxic agent. The objective of the study was to fractionate proteins based on solubility and assess its haemgglutinating activity. Protein fractionation was carried out using different solvent such as aqueous, 1.0 M Nacl, 70% ethanol and 0.2% NaOH to extract albumin, globulin, prolamin and glutelins respectively.. The amount of proteins was quantitatively measured. The result of protein fractionation indicated increase in glutelin and decrease in albumin content. The obtained protein fractions were used for determining hemagglutination activity. Agglutination was observed in prolamin fractions and not for the other fractions.

Selected Bioinformatic Tools and MS (MALDI-TOF, PMF) Techniques Used in the Strategy for the Identification of Oat Proteins After 2-DE.

Computer analysis of protein maps obtained from the separation of proteins with two-dimensional polyacrylamide gel electrophoresis (2-DE), in combination with mass spectrometry (MS) analysis and selected bioinformatic tools is used in the strategy for the identification of oat proteins. In proteomic research the most often used MS technique is the combination of ion sources: matrix-assisted laser desorption/ionization (MALDI) and the analyzer of the time of flight (TOF), i.e., MALDI-TOF MS.This chapter describes the possibilities of the use of selected bioinformatic tools (UniProtKB database, ProtParam, Compute pI/MW programs) for initial identification of separated oat proteins (especially prolamin fractions) with the 2-DE technique. Also the procedure of preparation of samples obtained from cut out protein spots for analysis with the MALDI-TOF MS and peptide mass fingerprinting (PMF) technique is presented.Among oat prolamins separated with the 2-DE technique (see Chapter 17 ), 13 protein spots are considered to be the most characteristic (range of MW 27.0-34.6 kDa, pI 5.7-7.6) for this fraction of proteins. Among them there are four protein spots (MW 27.0-28.0 kDa) and two spots (MW 31.4-32.1 kDa) which can correspond to avenins (Accession numbers (AC) in UniProtKB: L0L5I0, I4EP88, I4EP64, L0L4I8 and F2Q9W5, L0L6J0, respectively).

Isolation of Oat (Avena sativa L.) Total Proteins and Their Prolamin Fractions for 2D Electrophoresis.

Appropriate sample preparation is essential to obtaining good results of two-dimensional gel electrophoresis (2-DE). For various reasons (particularly phenolic compounds, proteolytic enzymes, and cell-wall mucilages) the extraction of proteins from plant material, among them oat proteins, is difficult. During isolation all soluble substances that may interfere with the analysis (especially isoelectric focusing) are removed, and proteins of interest are separated from the remains. However, the applied procedure of isolation cannot be too extensive, because additional stages cause loss of the proteins.In this chapter, we describe a simple procedure for the isolation of oat total proteins and their prolamin fractions prior to 2-DE, without necessity of considerable purification. It can be used for oat protein fractionation, measurement of oat protein concentration, and their 2-DE analysis, with particular reference to prolamin fractions. The presented routine includes modified methods of plant seed proteins extraction and sequential Osborne extraction, based on oat protein solubility differences.

2-DE Separation and Identification of Oat (Avena sativa L.) Proteins and Their Prolamin Fractions.

At present two-dimensional polyacrylamide gel electrophoresis (2-DE) is the most widely used proteomic tool, which enables simultaneous separation of even thousands of proteins with a high degree of resolution. The quality of 2-DE separation depends on the type of biological material used as a protein source. The presence of interfering compounds (e.g., phenols, as it is the fact in plant material including oat seeds) impedes 2-DE run. With the use of this technique it is possible to analyze the complex protein mixtures, characteristic protein fractions, as well as individual proteins.The purpose of this chapter is to describe the 2-DE technique (the separate stages of the first and the second dimension) for determining the oat protein composition (oat seed proteome), separation and preliminary identification of oat prolamin fractions. Electrophoretically separated proteins are identified on the basis of pI markers (identifying the location of both ends of an IPG strip) and on 2D SDS-PAGE standards. The gel images of oat proteins are analyzed with the help of ImageMaster 2D Platinum 6.0 program (Amersham Bioscience, part of GE Healthcare, Uppsala, Sweden). It allows finding unique spot identifiers for the occurrence of oat prolamin fractions in oat total proteins. The characteristic spots of similar shape and intensity (anchoring spots) and characteristic groups of spots can be searched for the purpose of identification.

Changes in Soluble Protein Fractions of Rice Varieties after Cooking by Different Methods

The aim of this research was to study the changes in soluble protein fractions of six rice varieties cooked by four cooking methods viz. ordinary, pressure, microwave and solar cooking methods. In cooked rice albumin, globulin, prolamin and glutelin fractions ranged from 4.1 to 4.3, 11.6 to 12.2, 3.0 to 3.6 and 80.5 to 81.0 % under various cooking methods against 6.4, 14.6, 4.6 and 74.4 % in the uncooked samples. Results indicated that albumin, globulin and prolamin fractions decreased significantly after cooking. This decrease was accompanied by a significant increase in the glutelin fraction as compared to uncooked rice samples. Among cooking methods, albumin in pressure and solar, globulin in solar and prolamin in ordinary were significantly (P&amp;lt;0.05) higher than other methods. However, in respect of glutelin content microwave and solar cooking methods were superior to ordinary but at par to pressure cooking method.

Cereals and Legumes in Nutrition of People with Celiac Disease

Cereals and legumes rank among the most important group of crop plant production. The aim of this paper was to point out the suitability of cereals and legumes in the diet of people living with an autoimmune disease of the small intestine, the celiac disease. Cereals match the best current ideas of healthy and balanced diet and provide decisive part of the energy intake from food in human nutrition and no small share from the total protein intake. Some cereals contain celiac active polypeptides and in susceptible individuals cause allergic reactions. Celiac active ingredients are found in the prolamin fraction. If the content of prolamine is in an amount of 4-8%, the products can be considered appropriate for the celiac diet. Wheat, barley, rye and oat should be excluded from the diet, if a person has confirmed celiac disease. On a worldwide basis, legumes contribute to about one-third of humankind's direct protein intake. Legumes also accumulate natural products (secondary metabolites) such as isoflavonoids that are considered beneficial to human health through anticancer and other health-promoting activities. The biggest advantage of legumes is that they are gluten-free and are suitable for gluten-free diet.

Impact of the preparation procedure on gliadin, glutenin and gluten contents of wheat starches determined by RP-HPLC and ELISA

Celiac disease patients rely on safe gluten-free products, and the use of purified wheat starch (WSt) as part of the diet is usually well tolerated. However, uncertainties about residual gluten amounts in WSt remain, because ELISAs target the alcohol-soluble prolamin (gliadin) fraction of gluten, but hardly detect the alcohol-insoluble glutelin (glutenin) fraction. Therefore, gliadin, glutenin and gluten contents of WSt prepared from doughs on a laboratory scale were monitored by RP-HPLC. WSt washed with water from optimally or overmixed doughs had the lowest gluten contents. Gliadins were removed more extensively than glutenins during consecutive washing steps, so that gluten contents analyzed by ELISA were lower than those by RP-HPLC in 17 out of 24 WSt samples. The inability to detect glutelins by ELISA may thus lead to an underestimation of gluten contents in WSt. These findings highlight the need for improved analytical methods capable of detecting both prolamins and glutelins in processed food samples.

Identification and molecular characterization of oat peptides implicated on coeliac immune response

BackgroundOats provide important nutritional and pharmacological properties, although their safety in coeliac patients remains controversial. Previous studies have confirmed that the reactivity of the anti-33-mer monoclonal antibody with different oat varieties is proportional to the immune responses in terms of T-cell proliferation. Although the impact of these varieties on the adaptive response has been studied, the role of the dendritic cells (DC) is still poorly understood. The aim of this study is to characterize different oat fractions and to study their effect on DC from coeliac patients.Methods and resultsProtein fractions were isolated from oat grains and analyzed by SDS–PAGE. Several proteins were characterized in the prolamin fraction using immunological and proteomic tools, and by Nano-LC-MS/MS. These proteins, analogous to α- and γ-gliadin-like, showed reactive sequences to anti-33-mer antibody suggesting their immunogenic potential. That was further confirmed as some of the newly identified oat peptides had a differential stimulatory capacity on circulating DC from coeliac patients compared with healthy controls.ConclusionsThis is the first time, to our knowledge, where newly identified oat peptides have been shown to elicit a differential stimulatory capacity on circulating DC obtained from coeliac patients, potentially identifying immunogenic properties of these oat peptides.

Targeted modification of storage protein content resulting in improved amino acid composition of barley grain.

C-hordein in barley and ω-gliadins in wheat are members of the prolamins protein families. Prolamins are the major component of cereal storage proteins and composed of non-essential amino acids (AA) such as proline and glutamine therefore have low nutritional value. Using double stranded RNAi silencing technology directed towards C-hordein we obtained transgenic barley lines with up to 94.7% reduction in the levels of C-hordein protein relative to the parental line. The composition of the prolamin fraction of the barley parental line cv. Golden Promise was resolved using SDS-PAGE electrophoresis, the protein band were excised and the proteins identified by quadrupole-time-of-flight mass spectrometry. Subsequent SDS-PAGE separation and analysis of the prolamin fraction of the transgenic lines revealed a reduction in the amounts of C-hordeins and increases in the content of other hordein family members. Analysis of the AA composition of the transgenic lines showed that the level of essential amino acids increased with a concomitant reduction in proline and glutamine. Both the barley C-hordein and wheat ω-gliadin genes proved successful for RNAi-gene mediated suppression of barley C-hordein level. All transgenic lines that exhibited a reduction for C-hordein showed off-target effects: the lines exhibited increased level of B/γ-hordein while D-hordein level was reduced. Furthermore, the multicopy insertions correlated negatively with silencing.

Targeting of prolamins by RNAi in bread wheat: effectiveness of seven silencing-fragment combinations for obtaining lines devoid of coeliac disease epitopes from highly immunogenic gliadins.

Gluten proteins are responsible for the viscoelastic properties of wheat flour but also for triggering pathologies in susceptible individuals, of which coeliac disease (CD) and noncoeliac gluten sensitivity may affect up to 8% of the population. The only effective treatment for affected persons is a strict gluten-free diet. Here, we report the effectiveness of seven plasmid combinations, encompassing RNAi fragments from α-, γ-, ω-gliadins, and LMW glutenin subunits, for silencing the expression of different prolamin fractions. Silencing patterns of transgenic lines were analysed by gel electrophoresis, RP-HPLC and mass spectrometry (LC-MS/MS), whereas gluten immunogenicity was assayed by an anti-gliadin 33-mer monoclonal antibody (moAb). Plasmid combinations 1 and 2 downregulated only γ- and α-gliadins, respectively. Four plasmid combinations were highly effective in the silencing of ω-gliadins and γ-gliadins, and three of these also silenced α-gliadins. HMW glutenins were upregulated in all but one plasmid combination, while LMW glutenins were downregulated in three plasmid combinations. Total protein and starch contents were unaffected regardless of the plasmid combination used. Six plasmid combinations provided strong reduction in the gluten content as measured by moAb and for two combinations, this reduction was higher than 90% in comparison with the wild type. CD epitope analysis in peptides identified in LC-MS/MS showed that lines from three plasmid combinations were totally devoid of CD epitopes from the highly immunogenic α- and ω-gliadins. Our findings raise the prospect of breeding wheat species with low levels of harmful gluten, and of achieving the important goal of developing nontoxic wheat cultivars.

Physico-chemical properties of globular tiger nut proteins

This study investigates the properties of globular tiger nut proteins by determining the average molecular mass, protein fractions, denaturation temperature and the isoelectric point. Tiger nut proteins (TNP) prepared by aqueous extraction had a purity of 83.5 % w/w on dry mass. Fractionation of TNP revealed that glutelin was the constituent with the highest concentration (>47.5 % w/w), followed by albumin (31.8 %), globulin (4.7 %) and prolamin (3.8 %). A residual protein fraction of 12.2 % appeared as electrophoretically similar to glutelin. TNP had an apparent molecular mass (m m) of 5.3–88 kDa. Both albumin and globulin fractions had m m of 5.3–73 kDa, whilst prolamin and glutamine fractions were 5.3–46.2 and 5.3–30 kDa, respectively. TNP had an onset temperature (T o), denaturation temperature (T d) and enthalpy of transition (∆H) of 54.40, 69.61 °C and 5.43 J/g, respectively. In decreasing order of T o and T d among the protein fractions were prolamin, albumin, globulin and glutelin. Albumin and glutelin showed the highest and lowest ∆H, respectively. Finally, the isoelectric point of TNP was 4.90. Fundamentally, the properties of TNP show that they might be useful for the techno-functional application in tiger nut-based food systems.

Nutritional, chemical and microbiological changes during fermentation of tarhana formulated with different flours.

BackgroundTarhana is a fermented cereal product that is used for the preparation of one of the favourite soups in Turkish cuisine. Tarhana is a mixture of wheat flour, yoghurt, baker’s yeast, salt, and various vegetables, spices and seasonings. It is obtained by mixing all ingredients in the recipe and afterwards the mixture is let to ferment at room temperature. Following fermentation tarhana is dried or frozen for long term storage. In this study, to improve the nutritional benefits of tarhana, whole wheat and chickpea flours were used as the sole source of flour. The changes in the phytic acid content, proteins and fermentation products were investigated in addition to some microbiological and chemical characteristics.ResultsThe effect of flour type on the phytic acid content was significant. No differences were observed in the glutenin band patterns of the wheat and whole wheat flours and their tarhana samples. Conversely, for the gliadin fractions, the bands of the wheat and whole wheat flours were more intense than their tarhana samples. The changes in the glutelin and prolamin fractions of the chickpea flour and the resultant tarhana dough were similar to the glutenin and gliadin fractions of wheat and whole wheat flours and their tarhana samples. In all samples, the yeasts displayed an undulant growth pattern and the effect of flour type and fermentation time on yeast growth was significant (P < 0.01). The effect of flour type (P < 0.01) and fermentation time (P < 0.05) on mesophilic LAB was significant. Similar behaviours were observed with the mesophilic LAB in all samples and their numbers remained closed to their initial numbers. The growth of thermophilic LAB was not influenced by the flour type, but the effect of fermentation time was significant (P < 0.01).ConclusionsThe whole wheat and chickpea tarhana are found to be good alternatives to classical tarhana with their higher nutritional benefits but further investigations are needed for the assessment of their sensory properties.