Emerging forward osmosis and membrane distillation for liquid food concentration: A review.

As emerging membrane technologies, forward osmosis (FO) and membrane distillation (MD), which work with novel driving forces, show great potential for liquid food concentration, owing to their low fouling propensity and great driving force. In the last decades, they have attracted the attention of food industry scientists in global scope. However, discussions of the FO and MD in liquid food concentration advancement, membrane fouling, and economic assessment have been scant. This review aims to provide an up-to-date knowledge about liquid food concentration by FO and MD. First, we introduce the principle and applications of FO and MD in liquid food concentration, and highlight the effect of process on liquid food composition, membrane fouling mechanism, and strategies for fouling mitigation. Besides, economic assessment of FO and MD processes is reviewed. Moreover, the challenges as well as future prospects of FO and MD applied in liquid food concentration are proposed and discussed. Comparing with conventional membrane-based or thermal-based technologies, FO and MD show outstanding advantages in high concentration rate, good concentrate quality, low fouling propensity, and low cost. Future efforts for liquid food concentration by FO and MD include (1) development of novel FO draw solution (DS); (2) understanding the effects of liquid food complex compositions on membrane fouling in FO and MD concentration process; and (3) fabrication of novel membranes and innovation of membrane module and process configuration for liquid food processing.

Structure and Function of Mung Bean Protein-Derived Iron-Binding Antioxidant Peptides.

An iron-binding mung bean protein hydrolysate (MBPH) was prepared using a continuous enzymatic membrane reactor followed by peptide separation on anion-exchange (AEC) and reverse-phase HPLC (RP-HPLC) columns. Amino acid sequences of peptides present in the RP-HPLC fraction with the strongest iron-binding capacity were identified using mass spectrometry, and ten peptides of 5-8 amino acids synthesized for antioxidant characterization. Five fractions (AF1- AF5) with higher iron-binding capacity (88.86 ± 6.43 to 153.59 ± 2.18 mg/g peptide) when compared to the MBPH (36.81 ± 0.93 mg/g peptide) were obtained from AEC. PAIDL had the significantly (p < 0.05) highest iron-binding capacity, but LLLLG and LLGIL showed the strongest metal chelating activity. However, PAIDL (46.63%) and LLGIL (81.27%) had significantly (p < 0.05) better DPPH radical scavenging activity than the other peptides. PAIDL and LLGIL were also the most effective (p < 0.05) hydroxyl radical neutralizers with an effective concentration that scavenged 50% (EC50) values of 0.09 and 0.37 mM, respectively. PAIDL and AIVIL showed the lowest EC50 values of 0.07 mM each for superoxide radical scavenging activity. We conclude that short chain length in combination with leucine as the C-terminal amino acid residue contributed to the strong antioxidant properties of peptides in this study.

Athermal forward osmosis process for the concentration of liquid egg white: Process performance and improved physicochemical property of protein.

The concentrated liquid egg white (LEW) by dewatering process displays the remarkable advantages. However, the concentration process was hindered by the high viscosity and heat sensitivity of LEW. Forward osmosis (FO) as an emerging membrane technology to concentrate LEW was evaluated for the first time in this study. The effects of process conditions on FO flux, fouling control, and product quality were investigated. The LEW can be concentrated up to about 2.1 folds by a single FO process. Flux decline (up to 80%) occurred during the process which was attributed to membrane fouling and dilution of draw solution. However, the membrane fouling could be mitigated by higher cross-flow velocity and the flux could be recovered up to 100% by osmotic backwash. There was no significant leakage of draw solutes and loss of protein in LEW during FO process. The concentration of LEW resulted in a promoted products quality.

Angiotensin I-converting enzyme inhibitory peptides produced from tuna cooking juice hydrolysate by continuous enzymatic membrane reactor.

Angiotensin I-converting enzyme (ACE) inhibitory peptides were derived from tuna cooking juice (TCJ) hydrolysis by alcalase in the continuous enzymatic membrane reactor (cEMR) coupling with 1 kDa MWCO membrane. The permeated sample from cEMR for 510 min of hydrolysis was purified by size exclusion chromatography in Sephadex G-25 column. A fraction exhibited the highest ACE inhibitory activity was further separated by RP-HPLC, resulting two fractions showed highest ACE inhibitory activities. The molecular weight (MW) and amino acid sequences of peptides from both fractions were determined using LC-MS/MS. Two potential ACE inhibitory peptides were obtained and showed molecular weight of 959.46 and 1,141.29 Da. PRACTICAL APPLICATIONS: Tuna cooking juice (TCJ) usually was either used as protein source of feed meal or directly discharged to wastewater treatment system. However, it contains water-soluble proteins in a group of sarcoplasmic protein, which is small water-soluble proteins and easily hydrolyzed to small peptides. In this study, the active peptides, angiotensin I-converting enzyme inhibitory peptides (MW of 959.46 and 1,141.29 Da), obtained from TCJ hydrolysate and identified by LC-MS/MS would be a beneficial ingredient for nutraceuticals and functional food against hypertension.

Anti-allergic activity of mung bean (Vigna radiata (L.) Wilczek) protein hydrolysates produced by enzymatic hydrolysis using non-gastrointestinal and gastrointestinal enzymes.

Mung bean seed is a well-known plant protein consumed in Asian countries but the protein is usually retrieved as a waste product during starch production. This study investigated the anti-allergic property of mung bean protein hydrolysates (MBPH) produced by enzymatic hydrolysis using non-gastrointestinal (non-GI), GI and a combination of non-GI+GI enzymes. The hydrolysates were investigated for any anti-allergic property by detecting the amount of ß-hexosaminidase released in RBL-2H3 cells, and complemented with the MTT assay to show cell viability. It was found that MBPH hydrolyzed by a combination of flavourzyme (non-GI enzyme) and pancreatin (GI enzyme) exhibited the highest anti-allergic activity (135.61%), followed by those produced with alcalase, a non-GI enzyme (121.74%) and 80.32% for pancreatin (GI enzyme). Minimal toxicity (<30%) of all hydrolysates on RBL-2H3 cells line was observed. The results suggest that MBPH can potentially serve as a hypoallergenic food ingredient or supplement. PRACTICAL APPLICATIONS: Mung bean (Vigna radiata L. (Wilczek)) is also known as "green gram" and it is an excellent source of protein. The major mung bean storage proteins are the globulin, albumin and legumin, which are also referred to as legume allergens. Our study showed that mung bean peptides obtained after enzymatic hydrolysis influenced ß-hexosaminidase inhibition without any toxic effect on RBL-2H3 cells. This indicates that mung bean allergenicity can be reduced after enzymatic hydrolysis and the protein hydrolysates could be as a hypoallergic food, ingredient, supplement and/or protein substitute in the formulation of food products.

Influence of gas-liquid two-phase flow on angiotensin-I converting enzyme inhibitory peptides separation by ultra-filtration.

BACKGROUND: Membrane fouling is a major problem in ultra-filtration systems and two-phase flow is a promising technique for permeate flux enhancement. The objective of this research was to study the use of an ultra-filtration (UF) system to enrich angiotensin-I converting enzyme (ACE) inhibitory peptides from tilapia protein hydrolysate. To select the most appropriate membrane and operating condition, the effects of membrane molecular weight cut-off (MWCO), transmembrane pressure (TMP) and cross-flow velocity (CFV) on permeate flux and ACE inhibitory peptide separation were studied. Additionally, the gas-liquid two-phase flow technique was applied to investigate its effect on the process capability. RESULTS: The results showed that the highest ACE inhibitory activity was obtained from permeate of the 1 kDa membrane. In terms of TMP and CFV, the permeate flux tended to increase with TMP and CFV. The use of gas-liquid two-phase flow as indicated by shear stress number could reduce membrane fouling and increase the permeate flux up to 42%, depending on shear stress number. Moreover, the use of a shear stress number of 0.039 led to an augmentation in ACE inhibitory activity of permeates. CONCLUSIONS: Operating conditions using a shear stress number of 0.039 were recommended for enrichment of ACE inhibitory peptides. © 2016 Society of Chemical Industry.

Triple helical structure of acid-soluble collagen derived from Nile tilapia skin as affected by extraction temperature.

BACKGROUND: Fish skin has become a new source of collagen. It is usually extracted at low temperature. Increasing the extraction temperature can increase the collagen yield. However, high temperature might cause degradation of the triple helical structure of collagen, which is related to its functional biomaterial. This work thus aimed to investigate the effect of extraction temperature on the extraction efficiency and characteristics of acid-soluble collagen (ASC), particularly its triple helical structure. RESULTS: ASC was extracted at 5 ± 1, 15 ± 1 and 25 ± 1 °C for 0-24 h with 0.3 or 0.5 mol L(-1) acetic acid. The results showed that extraction with 0.5 mol L(-1) acetic acid gave a higher extraction efficiency than that in 0.3 mol L(-1) acetic acid (P < 0.5). Extraction at 25 ± 1 °C for 5 h with 0.5 mol L(-1) acetic acid gave a higher extraction efficiency (73.73 ± 1.28%), which is higher than that of 5 ± 1 °C by about 1.7-fold. All ASC obtained were identified as type I collagen and showed similar physicochemical properties. CONCLUSION: The results showed that extraction temperature strongly affected extraction efficiency. Extraction at 25 °C did not affect the triple helical structure, which was confirmed by the results of Fourier transform infrared, circular dichroism spectrum and collagen self-assembly. © 2015 Society of Chemical Industry.

Separation of proteases from yellowfin tuna spleen by ultrafiltration.

Separation of protease, trypsin and chymotrypsin from yellowfin tuna spleen extract by ultrafiltration (UF) using regenerated cellulose membranes with molecular weight cut off (MWCO) 30 and 100 kDa was studied. The 100 kDa membrane had a higher transmission of enzymes than that of the 30 kDa membrane. The enzyme transmission varied from 0.01 to 0.18 and from 0.6 to 0.8 for the 30 kDa membrane and 100 kDa membrane, respectively. The protein transmission was about 0.8 for both membranes. Increasing cross-flow rate and transmembrane pressure (TMP) increased permeate flux. The limiting fluxes at cross-flow rate 120, 240 and 360 L/h for the 30 kDa membrane were 17.3, 43.9 and 54.7 L/m2h, respectively and the limiting fluxes at the same flow rate for 100 kDa membrane were 34.1, 51.1 and 68.4 L/m2h, respectively. The separation of these proteases was achieved using the 30 kDa membrane. The purities of proteases were increased more than ten times at TMP 1.5 bar and cross-flow rate 360 L/h by diafiltration using 30 kDa membrane.

Effect of hydrodynamic and physicochemical changes on critical flux of milk protein suspensions.

The critical flux during ultrafiltration of whey protein concentrate and sodium caseinate suspensions was investigated. The weak form of critical flux was found for both suspensions. Critical flux of sodium caseinate was higher than that of whey protein concentrate. This could be due to the differences in particle size of the suspensions, resulting in a slower particle back transportation for small particles (whey proteins) compared to the larger casein micelles. Critical flux increased as crossflow velocity increased and decreased as concentration increased, suggesting that critical flux was determined by competition between rate of particle removal from the membrane surface and rate of particle movement towards the membrane surface. Influence of changing pH, addition of NaCl and CaCl2 on the critical fluxes of both protein suspensions was also studied. Increasing pH led to an increase in critical flux for both protein suspensions, suggesting that electrostatic repulsive forces are involved in determining critical flux in both cases. Addition of NaCl gave rise to a decrease in electrostatic interactions due to an increase in ionic strength and zeta potential, and resulted in a decrease in critical flux for sodium caseinate, but had no significant effect for whey protein concentrate. Addition of CaCl2 resulted in a decrease in the critical flux and had a more pronounced influence than NaCl. These results suggest that, in addition to electrostatic repulsive forces, other factors such as structure of protein may be involved in determining the critical flux.