Valorization of different low-grade date (Phoenix dactylifera L.) fruit varieties: A study on the bioactive properties of polyphenolic extracts and their stability upon in vitro simulated gastrointestinal digestion.

Nowadays, the development of suitable strategies for the management and valorization of agri-food products is one of the most important challenges worldwide. In this context, the current research study aimed to explore a valorization strategy for different varieties (Khalas, Jabri, Lulu, Booman, and Sayer) of low-grade date fruit by extracting polyphenolic compounds and investigating their health-promoting bioactive properties. The generated extracts were comparatively analyzed for their phenolic contents, antioxidant, anti-inflammatory, anti-hemolytic, and enzyme inhibitory activities upon in vitro simulated gastrointestinal digestion (SGID). The total phenolic contents (TPC) ranged from 217.3 to 1846.9 mg GAE/100 g fresh weight. After complete SGID, the TPC remarkably increased from 570.8 mg GAE/100 g fresh weight (undigested), reaching the highest value of 1606.3 mg GAE/100 g fresh weight with the Khalas cultivar. Overall, gastric and complete-SGID-treated extracts exhibited higher antioxidant activities, compared to the undigested extracts for the five selected date varieties. Similarly, the gastric and complete SGID promoted the release of bioactive components endowed with significantly higher inhibition levels towards digestive enzymes related to diabetes. Moreover, extracts from all varieties revealed an increase in the inhibition of lipidemic-related enzymatic markers and anti-inflammatory activities when subjected to the gastric digestion phase, which decreased after complete SGID. Principal component analysis (PCA) suggested that higher bioactive properties were influenced by the TPC present in the samples. Overall, low-quality dates could be considered as a potential source of bioactive polyphenols with interesting nutraceutical properties, released upon their transit through the gastrointestinal tract.

Green solvent processing: Effect of type of solvent on extraction and quality of protein from dairy and non-dairy expired milk products.

The present study was designed to study the effect of green solvent processing in two folds, (i) to extract valuable protein from dairy and non-dairy expired milk products and (ii) to compare extraction efficiency and quality of extracted protein using conventional (CS) and green solvents (GS). Ethyl acetate, ethanol, isopropanol, n-heptane and cyclopentyl methyl ether (CPME) were selected as the GS for the possible substitution of hexane and ethyl ether. For each respective solvent, protein recovery, structural and functional modifications were studied. Protein yield was extracted most effectively by GS n-heptane in dairy milk (5.33 ± 0.01%) with a protein purity of 39.73 ± 0.90%. Non-dairy milk and product had similar protein yield when treated with CS and GS. Total mean of extraction efficiency, structural and functional modifications across all samples showed GS solvents were statistically more effective than CS.

A comparative analysis of anti-lipidemic potential of soybean (Glycine max) protein hydrolysates obtained from different ripening stages: Identification, and molecular interaction mechanisms of novel bioactive peptides.

This study aims to investigate the potentials of mature (MSPHs) and young (YSPHs) soybean enzymatic protein hydrolysates for the inhibition of pancreatic lipase (PL) and cholesterol esterase (C-Ease) enzymes. Higher proteins degradation levels were recorded with Bromelain compared to Flavourzyme and Alcalase, and upon hydrolysis, improved PL and C-Ease inhibition performances were displayed compared to unhydrolyzed proteins. Afterwards, six PHs with potent anti-lipidemic activities were selected for sequencing using LC-MS QTOF and molecular binding studies. Peptides FPFPRPPHQ, QCCAFEM, FAPEFLK from MSPHs and SFFFPFELPRE, FMYL, PFLL, FPLL, LPHF from YSPHs were predicted to possess potent inhibitory activities against PL. Furthermore, FPFPRPPHQ, FMYL, MMLM from MSPHs, and SFFFPFELPRE from YSPHs were predicted to be potent inhibitors of C-Ease. FPFPRPPHQ and SFFFPFELPRE derived from MSPHs and YSPHs, respectively, demonstrated effective inhibition potentialities against both PL and C-Ease. Therefore, mature and young soybean-derived protein hydrolysates could be recognized as a potential ingredient in the management of hypercholesterolemia.

Multifunctional bioactive properties of hydrolysates from colocynth (Citrullus colocynthis) seeds derived proteins: Characterization and biological properties.

Citrullus colocynthis (Colocynth) has gained a great deal of interest in their applications as indigenous nutraceutical and as a functional food ingredient. The intact colocynth seed protein was enzymatically hydrolyzed using proteolytic enzymes (alcalase, bromelain, and chymotrypsin) at different time intervals of 3, 6, and 9 h. The highest degree of hydrolysis (87.82%) was observed in chymotrypsin derived colocynth seed protein hydrolysates (CSPH) for 9 h. The CSPHs was further investigated through in-vitro assay to explore its potential biological activity such as antioxidant, inhibition of enzymatic marker related to diabetes (DPP-IV, α-glucosidase and α-amylase) and hyperlipidaemia (cholesteryl esterase and pancreatic lipase). Chymotrypsin hydrolysate showed the strongest DPPH (65.7 mM TEAC) and ABTS (525.2 mM TEAC) radical scavenging activity after 6 h of hydrolysis. Moreover, chymotrypsin-treated CSPH for 6 h inhibited cholesteryl esterase (IC50 = 13.68 µg/mL) and pancreatic lipase (IC50 = 14.12 µg/mL) significantly when compared to native protein. Whereas, bromelain and alcalase treated hydrolysate for 6 h effectively inhibited α-glucosidase and α-amylase at an inhibitory concentration of IC50 = 13.27 µg/mL and of IC50 = 17 µg/mL. Overall, the findings indicated that protein hydrolysates exhibited superior biological activity than intact colocynth seed proteins isolate (CSPI) and could be a sustainable source of bioactive peptides.

Impact of cavitation on the structure and functional quality of extracted protein from food sources - An overview.

Increasing protein demands directly require additional resources to those presently and recurrently available. Emerging green technologies have witnessed an escalating interest in "Cavitation Processing" (CP) to ensure a non-invasive, non-ionizing and non-polluting extraction. The main intent of this review is to present an integrated summary of cavitation extraction methods specifically applied to food protein sources. Along with a comparative assessment carried out for each type of cavitation model, protein extraction yield and implications on the extracted protein's structural and functional properties. The basic principle of cavitation is due to the pressure shift in the liquid flow within milliseconds. Hence, cavitation emerges similar to boiling; however, unlike boiling (temperature change), cavitation occurs due to pressure change. Characterization and classification of sample type is also a prime candidate when considering the applications of cavitation models in food processing. Generally, acoustic and hydrodynamic cavitation is applied in food applications including extraction, brewing, microbial cell disruption, dairy processing, emulsification, fermentation, waste processing, crystallisation, mass transfer and production of bioactive peptides. Micro structural studies indicate that shear stress causes disintegration of hydrogen bonds and Van der Waals interactions result in the unfolding of the protein's secondary and/or tertiary structures. A change in the structure is not targeted but rather holistic and affects the physicochemical, functional, and nutritional properties. Cavitation assisted extraction of protein is typically studied at a laboratory scale. This highlights limitations against the application at an industrial scale to obtain potential commercial gains.

Nutraceutical and bioactive potential of high-quality date fruit varieties (Phoenix dactylifera L.) as a function of in-vitro simulated gastrointestinal digestion.

The present study aims to investigate the digestive process (gastric and intestinal phases) effects on the survivability of total and individual phenolic compounds, and the in vitro health-related bioactive properties of four high-quality and commonly consumed dates (Phoenix dactylifera) varieties (Safawi, Khalas, Khudri, and Booman). Phenolic compounds were analyzed by HPLC-UV (at 275 nm) and a higher amount of phenolics were identified in Khalas and Booman intestinal digested extracts, compared to the other date varieties-based extracts, which corroborates with the total phenolic contents in those samples, with respective values of 186.5 and 358.14 mg GAE/100 g. Considering their bioactive potentialities, the highest DPPH radical scavenging activities, of around 320 TEAC µg/mL, were observed with Khalas and Khudri gastric extracts. In contrast, Khalas intestinal extract displayed the highest ABTS radical scavenging potential of 969 TEAC µg/mL. Moreover, the Safawi intestinal extract, along with Khalas and Booman gastric extracts, showed the highest increase in the α-glucosidase inhibition activity, compared to the other date varieties-based extracts. Safawi and Khalas intestinal extracts displayed the highest DPP-IV inhibition activities (IC50 of 2.85 µg/mL). Additionally, regarding the pancreatic lipase and cholesterol esterase inhibition, Khudri and Khalas varieties after intestinal digestion demonstrated the highest activities. These results suggested that the Khalas variety showed more potent bioactive properties than other date varieties, mainly related to the variations in the phenolic content between date varieties. Overall, this study provides additional insight into investigating these dates varieties upon their simulated gastro-intestinal digestion and exhibition of multifunctional bioactive properties.

Camel whey protein with enhanced antioxidative and antimicrobial properties upon simulated gastro-intestinal digestion.

Background: Whey proteins and their peptide derivatives have attracted a great attention of researchers in the pharmaceutical and nutritional fields, due to their numerous bio-functionalities. Aim: In the present research study, enzymatic protein hydrolysates (CWPHs) from camel whey proteins (CWPs) were produced and investigated for their antioxidant and antimicrobial potentials. Methods: Herein, Pepsin (gastric), and Trypsin and Chymotrypsin (pancreatic) enzymes were used to produce CWPHs. The obtained hydrolysates were characterize to ascertain the level of protein degradation and studies on their antimicrobial and antioxidant potential were conducted. Results: Among all CWPHs, a complete degradation of all different protein bands was perceived with Chymotrypsin-derived CWPHs, whereas, light bands of serum albumin and α-lactalbumin were observed with Trypsin and Pepsin-derived CWPHs. After enzymatic degradation, both CWPHs antioxidant and antimicrobial activities were improved. Chymotrypsin-derived CWPHs demonstrated higher DPPH and ABTS radical scavenging activities, anent the increase in proteolysis time. Compared to unhydrolyzed CWPs, higher metal chelating activities were displayed by Trypsin-derived CWPHs. No significant increase in the FRAP activities was noticed after CWPs hydrolysis using Trypsin and Chymotrypsin, while Pepsin-derived CWPHs showed higher reducing power. In terms of antimicrobial activity, significantly higher bacterial growth inhibition rates were exhibited by CWPHs compared to the unhydrolyzed CWP. Conclusion: Overall, CWPHs displayed enhanced antioxidative and antimicrobial properties.

A comparative investigation into novel cholesterol esterase and pancreatic lipase inhibitory peptides from cow and camel casein hydrolysates generated upon enzymatic hydrolysis and in-vitro digestion.

Cow (CwC) and camel casein (CaC) hydrolysates were generated using Alcalase™ (CwCA and CaCA) and Pronase-E (CwCP and CaCP) each for 3 and 6 h, and investigated for their potential to inhibit key lipid digesting enzymes i.e., pancreatic lipase (PL) and cholesteryl esterase (CE). Results revealed stronger PL and CE inhibition by CaC hydrolysates compared to CwC. Potent hydrolysates (CwCP-3 h and CaCA-6 h) upon simulated gastrointestinal digestion (SGID) showed significant improvement in inhibition of both PL and CE. However, both the SGID hydrolysates showed similar extent of PL and CE inhibition and were further sequenced for peptide identification. Peptides MMML, FDML, HLPGRG from CwC and AAGF, MSNYF, FLWPEYGAL from CaC hydrolysates were predicted to be most active PL inhibitory peptides. Peptide LP found in both CwC and CaC hydrolysates was predicted as active CE inhibitor. Thus, CwC and CaC could be potential source of peptides with promising CE and PL inhibitory properties.

Extraction of protein from food waste: An overview of current status and opportunities.

The chief intent of this review is to explain the different extraction techniques and efficiencies for the recovery of protein from food waste (FW) sources. Although FW is not a new concept, increasing concerns about chronic hunger, nutritional deficiency, food security, and sustainability have intensified attention on alternative and sustainable sources of protein for food and feed. Initiatives to extract and utilize protein from FW on a commercial scale have been undertaken, mainly in the developed countries, but they remain largely underutilized and generally suited for low-quality products. The current analysis reveals the extraction of protein from FW is a many-sided (complex) issue, and that identifies for a stronger and extensive integration of diverse extraction perspectives, focusing on nutritional quality, yield, and functionality of the isolated protein as a valued recycled ingredient.

Simulated gastrointestinal digestion of camel and bovine casein hydrolysates: Identification and characterization of novel anti-diabetic bioactive peptides.

Camel milk proteins are an important substrate for bioactive peptides generation. This study investigates in-vitro antidiabetic effect (via inhibition of α-amylase (AA), α-glucosidase (AG) and dipeptidyl peptidase IV (DPP-IV)) of bovine (BC) and camel casein (CC) hydrolysates. Further, effect of simulated gastrointestinal digestion (SGID) on inhibitory potential of generated hydrolysates was also explored. Both BC and CC hydrolysates displayed potent inhibitory properties against AA (IC50 value- 0.58 & 0.59 mg/mL), AG (IC50 value- 1.04 & 0.59 mg/mL) and DPP-IV (IC50 value- 0.62 & 0.66 mg/mL), respectively. Among different peptides identified in BC and CC hydrolysates, it was observed that FLWPEYGAL was predicted to be most potent inhibitory peptide against AA. While LPTGWLM, MFE and GPAHCLL as most active inhibitor of AG and HLPGRG, QNVLPLH and PLMLP were predicted to be active against DPP-IV. Overall, BC and CC hydrolysates can be proposed to be used in different food formulations as functional antidiabetic agents.

Identification and characterization of novel α-amylase and α-glucosidase inhibitory peptides from camel whey proteins.

This study explores the inhibitory properties of camel whey protein hydrolysates (CWPH) toward α-amylase (AAM) and α-glucosidase (AG). A general full factorial design (3 × 3) was applied to study the effect of temperature (30, 37, and 45°C), time (120, 240, and 360 min), and enzyme (pepsin) concentration (E%; 0.5, 1, and 2%). The results showed that maximum degree of hydrolysis was obtained when hydrolysis was carried out at higher temperature (45°C; P < 0.05), compared with lower temperatures of 30 and 37°C. Electrophoretic pattern displays degradation of all protein bands upon hydrolysis by pepsin at various hydrolysis conditions applied. All the 27 CWPH generated showed significant AAM and AG inhibitory potential as indicated by their lower IC50 values (mg/mL) compared with intact whey proteins. In total 196 peptides were identified from selected hydrolysates and 15 potential peptides (PepSite score > 0.8; http://pepsite2.russelllab.org/) were explored via in silico approach. Novel peptides PAGNFLMNGLMHR, PAVACCLPPLPCHM, MLPLMLPFTMGY, and PAGNFLPPVAAAPVM were identified as potential inhibitors for both AAM and AG due to their high number of binding sites and highest binding probability toward the target enzymes. CCGM and MFE, as well as FCCLGPVPP were identified as AG and AAM inhibitory peptides, respectively. This is the first study that reports novel AG and AAM inhibitory peptides from camel whey proteins. The future direction for this research involves synthesis of these potential AG and AAM inhibitory peptides in a pure form and investigate their antidiabetic properties in the in vitro, as well as in vivo models. Thus, CWPH can be considered for potential applications in glycaemic regulation.

Comparative characterization of protein and lipid fractions from camel and cow milk, their functionality, antioxidant and antihypertensive properties upon simulated gastro-intestinal digestion.

In-depth characterization of protein and lipid fractions from cow and camel milk (four breeds; CM-1 to 4), their functional and thermal properties and bioactivity upon simulated gastro-intestinal digestion was reported. Results revealed that proteins from cow and camel milk showed a noticeable separation on sodium dodecyl sulphate-polyacrylamide gel electrophoresis and high-performance liquid chromatography. Functional properties of whole milk proteins from cow and camel milk at different pH revealed that emulsifying activity index (EAI), foaming capacity (FC) and protein solubility was higher towards acidic and alkaline pH and lowest at isoelectric point (pH = 4). Moreover, the water absorption capacity (WAC) and solubility in water were higher in milk from cow (CW) compared to those from camel breeds (CM 1-4). Camel milk, which contains lower saturated and higher unsaturated fatty acids and demonstrated higher antioxidative and angiotensin-1 converting enzyme (ACE) inhibitory potential compared to cow milk upon simulated gastro-intestinal digestion, can be considered as a healthier option.

Inhibitory properties of camel whey protein hydrolysates toward liver cancer cells, dipeptidyl peptidase-IV, and inflammation.

This report describes an investigation of camel whey protein hydrolysates (CWPH) produced by gastric and pancreatic enzymes for their in vitro antidiabetic, anticancer, and anti-inflammatory properties. Degree of hydrolysis (DH) ranged from 8.54 to 47.53%, with hydrolysates generated using chymotrypsin for 6 h displaying the highest DH. Reverse phase-HPLC analysis showed that α-lactalbumin underwent complete degradation, with no intact α-lactalbumin detected in CWPH. The CWPH displayed enhanced antidiabetic activity compared with intact whey proteins; with pepsin- and chymotrypsin-generated CWPH displaying greater inhibition of dipeptidyl peptidase IV (DPP-IV), α-glucosidase, and α-amylase compared with trypsin-generated CWPH. The highest antiproliferative effect was observed for CWPH generated by chymotrypsin for 3 h, with only 4.5 to 6.5% viable liver cancer cells (HepG2) remaining when tested at concentrations from 400 to 1,000 µg/mL. The highest anti-inflammatory activity was manifested by CWPH generated by pepsin at 6-h hydrolysis. We report enhanced antiproliferative, antidiabetic, and anti-inflammatory activities upon hydrolysis of camel whey proteins, indicating their potential utilization as bioactive and functional ingredients.

Characterization and identification of novel antidiabetic and anti-obesity peptides from camel milk protein hydrolysates.

In-vitro inhibitory properties of peptides released from camel milk proteins against dipeptidyl peptidase-IV (DPP-IV), porcine pancreatic α-amylase (PPA), and porcine pancreatic lipase (PPL) were studied. Results revealed that upon hydrolysis by different enzymes, camel milk proteins displayed dramatic increase in inhibition of DPP-IV and PPL, but slight improvement in PPA inhibition was noticed. Peptide sequencing revealed a total of 20 and 3 peptides for A9 and B9 hydrolysates respectively, obtained the score of 0.8 or more on peptide ranker and were categorized as potential DPP-IV inhibitory peptides. KDLWDDFKGL in A9 and MPSKPPLL in B9 were identified as most potent PPA inhibitory peptide. For PPL inhibition only 7 and 2 peptides qualified as PPL inhibitory peptides from hydrolysates A9 and B9, respectively. The present study report for the first time PPA and PPL inhibitory and only second for DPP-IV inhibitory potential of protein hydrolysates from camel milk.

Production of functional pita bread using date seed powder.

Functional foods represent a novel approach to prevent diet-related diseases. Due to its excellent nutritional and antioxidant properties, date seed was used to develop functional pita bread. Flour was replaced by 5, 10, 15 and 20 % date seed powder. Regular and whole wheat pita breads were the references. Results clearly showed that date seed powder containing bread contained comparable dietary fibers levels as in whole wheat bread and higher levels of flavonoids and phenolics. Date seed powder containing breads were particularly rich in flavan-3-ols whereas reference breads did not contain any of them and only a limited amount of other phenolic compounds. They also exhibited a much higher antioxidant capacity. Additionally, compared to regular bread, acrylamide level was significantly lower in 5 % date seed powder containing bread, and lower in all date seed powder containing breads compared to whole wheat bread. Date seed powder supplemented bread appears as a promising functional ingredient to prevent chronic diseases.

Physicochemical and biochemical properties of honeys from arid regions.

This study was conducted to evaluate the quality of 11 honeys from arid regions for first time, and compare it with 5 different honeys from non-arid regions. Mean values obtained for physicochemical parameters were: pH 4.76 ± 0.55; 17.32 ± 1.8% moisture; 80.95 ± 1.60 °Brix sugar; 69.05 ± 4.41% total sugar; 413.81 ± 178.48 µS cm(-1) electrical conductivity; 17.58 ± 7.68 meq/kg free acidity; 11.05 ± 3.18 meq/kg lactonic acidity; 28.63 ± 9.6 meq/kg total acidity; 12.66 ± 20.39 mg/kg HMF; 0.58 ± 0.03 water activity; and 0.98 ± 0.62 colour intensity. Potassium was the major mineral (1760.54 ± 685.24 mg/kg). All the samples showed considerable significant variations with reference to their physicochemical and biochemical properties, moreover, the total free amino acids and total carotenoids were 61.13 ± 63.16 mg/100g and 4.07 ± 10.05 µg/100g respectively. Acrylamide was detected only in one sample at 2.39 ± 0.22 µg/kg.

Bioactive components, antioxidant and DNA damage inhibitory activities of honeys from arid regions.

Honey serves as a good source of natural antioxidants, which are effective in reducing the risk of occurrence of several diseases. This study was undertaken to address the limited knowledge regarding the polyphenolic content, antioxidant and DNA damage inhibitory activities of honeys produced in arid regions and compare them with well-recognized honeys from non-arid regions. Different types of honey were assessed for their contents of total phenolics, total flavonoids, and certain types of phenolic compounds. The antioxidant capacity of honey was evaluated by ferric-reducing/antioxidant power assay (FRAP), free radical-scavenging activity (DPPH), nitric oxide (NO) radical-scavenging assay, total antioxidant activity, and DNA damage. Results clearly showed significant differences among honeys with all the evaluated parameters. Results also showed that one or more types of honey from arid regions contained higher levels of phenolic compounds, free radical-scavenging activities, or DNA damage inhibitory activities compared with the evaluated honeys from non-arid regions.

Mitochondrial superoxide mediates labile iron level: evidence from Mn-SOD-transgenic mice and heterozygous knockout mice and isolated rat liver mitochondria.

Superoxide is the main reactive oxygen species (ROS) generated by aerobic cells primarily in mitochondria. It is also capable of producing other ROS and reactive nitrogen species (RNS). Moreover, superoxide has the potential to release iron from its protein complexes. Unbound or loosely bound cellular iron, known as labile iron, can catalyze the formation of the highly reactive hydroxyl radical. ROS/RNS can cause mitochondrial dysfunction and damage. Manganese superoxide dismutase (Mn-SOD) is the chief ROS-scavenging enzyme and thereby the primary antioxidant involved in protecting mitochondria from oxidative damage. To investigate whether mitochondrial superoxide mediates labile iron in vivo, the levels of labile iron were determined in the tissues of mice overexpressing Mn-SOD and heterozygous Mn-SOD-knockout mice. Furthermore, the effect of increased mitochondrial superoxide generation on labile iron levels was determined in isolated rat liver mitochondria exposed to various electron transport inhibitors. The results clearly showed that increased expression of Mn-SOD significantly lowered the levels of labile iron in heart, liver, kidney, and skeletal muscle, whereas decreased expression of Mn-SOD significantly increased the levels of labile iron in the same organs. In addition, the data showed that peroxidative damage to membrane lipids closely correlated with the levels of labile iron in various tissues and that altering the status of Mn-SOD did not alter the status of other antioxidant systems. Results also showed that increased ROS production in isolated liver mitochondria significantly increased the levels of mitochondrial labile iron. These findings constitute the first evidence suggesting that mitochondrial superoxide is capable of releasing iron from its protein complexes in vivo and that it could also release iron from protein complexes contained within the organelle.