Recovery of Nutrients from Cod Processing Waters.

Liquid side-streams from food industries can be processed and used in food applications and contribute to reduce the environmental footprint of industries. The goal of this study was to evaluate the effectiveness and applicability of protein and phosphorus separation processes, namely microfiltration, ultrafiltration and flocculation, using protein-rich process waters with low (LS) and high (HS) salt content from the processing of salted cod (Gadus morhua). The application of different flocculants (chitosan lactate and Levasil RD442) were evaluated at different concentrations and maturation periods (0, 1 or 3 h). The results showed that different flocculation treatments resulted in different recoveries of the nutrients from LS and HS. Proteins in LS could be most efficiently recovered by using Levasil RD442 0.25% and no maturation period (51.4%), while phosphorus was most efficiently recovered when using Levasil RD442 1.23% and a maturation period of 1 h (34.7%). For HS, most of its protein was recovered using Levasil RD442 1.23% and a maturation period of 1 h (51.8%), while phosphorus was recovered the most using Levasil 1.23% and no maturation period (47.1%). The salt contents allowed interactions through intermolecular forces with Levasil RD442. The ultrafiltration method was effective on HS since it recovered higher percentages of nutrients in the retentate phase (57% of the protein and 46% of the phosphorus) compared to LS.

Production of GABA-enriched idli with ACE inhibitory and antioxidant properties using Aspergillus oryzae: the antihypertensive effects in spontaneously hypertensive rats.

The present study aimed to develop a fermented food (idli) with enhanced γ-aminobutyric acid (GABA) and angiotensin I-converting enzyme (ACE) inhibitory properties using a GABA-producing fungus. Aspergillus oryzae NSK fermented idli batter and GABA was maximized (451.7 mg kg-1) in 120 h. The ACE inhibitory, 2,2-diphenyl-1-picryl-hydrazyl-hydrate (DPPH) free radical scavenging and nitric oxide radical scavenging activities increased to 41.8%, 1.9 and 0.6 µmol trolox equivalent antioxidant capacity (TEAC) per gram in 120 h, respectively. In contrast, phytic acid and trypsin inhibitor activities decreased to 3.01 g kg-1 and 30.8 mg kg-1, respectively. The systolic blood pressure of spontaneously hypertensive rats in the fermented idli diet group was lower than those fed a plain idli diet. Lipid peroxidation in the plain idli diet group was significantly higher, whereas superoxide dismutase and glutathione reductase activities were significantly lower. The expression of genes ET-1, HSP70, NF-κB and iNOS in the aorta of SHRs that received GABA-containing diets was down-regulated between 2.2 and 3.8 fold. The production of GABA-enriched foods can be a promising approach to lower the blood pressure of spontaneously hypertensive rats.

Enzyme Hydrolysates from Stichopus horrens as a New Source for Angiotensin-Converting Enzyme Inhibitory Peptides.

Stichopus horrens flesh was explored as a potential source for generating peptides with angiotensin-converting enzyme (ACE) inhibitory capacity using 6 proteases, namely alcalase, flavourzyme, trypsin, papain, bromelain, and protamex. Degree of hydrolysis (DH) and peptide profiling (SDS-PAGE) of Stichopus horrens hydrolysates (SHHs) was also assessed. Alcalase hydrolysate showed the highest DH value (39.8%) followed by flavourzyme hydrolysate (32.7%). Overall, alcalase hydrolysate exhibited the highest ACE inhibitory activity (IC(50) value of 0.41 mg/mL) followed by flavourzyme hydrolysate (IC(50) value of 2.24 mg/mL), trypsin hydrolysate (IC(50) value of 2.28 mg/mL), papain hydrolysate (IC(50) value of 2.48 mg/mL), bromelain hydrolysate (IC(50) value of 4.21 mg/mL), and protamex hydrolysate (IC(50) value of 6.38 mg/mL). The SDS-PAGE results showed that alcalase hydrolysate represented a unique pattern compared to others, which yielded potent ACE inhibitory peptides with molecular weight distribution lower than 20 kDa. The evaluation of the relationship between DH and IC(50) values of alcalase and flavourzyme hydrolysates revealed that the trend between those parameters was related to the type of the protease used. We concluded that the tested SHHs would be used as a potential source of functional ACE inhibitory peptides for physiological benefits.

Purification, characterization and thermal inactivation kinetics of a non-regioselective thermostable lipase from a genotypically identified extremophilic Bacillus subtilis NS 8.

Thermostable lipase produced by a genotypically identified extremophilic Bacillus subtilis NS 8 was purified 500-fold to homogeneity with a recovery of 16% by ultrafiltration, DEAE-Toyopearl 650M and Sephadex G-75 column. The purified enzyme showed a prominent single band with a molecular weight of 45 kDa. The optimum pH and temperature for activity of lipase were 7.0 and 60°C, respectively. The enzyme was stable in the pH range between 7.0 and 9.0 and temperature range between 40 and 70°C. It showed high stability with half-lives of 273.38 min at 60°C, 51.04 min at 70°C and 41.58 min at 80°C. The D-values at 60, 70 and 80°C were 788.70, 169.59 and 138.15 min, respectively. The enzyme's enthalpy, entropy and Gibb's free energy were in the range of 70.07-70.40 kJ mol(-1), -83.58 to -77.32 kJ mol(-1)K(-1) and 95.60-98.96 kJ mol(-1), respectively. Lipase activity was slightly enhanced when treated with Mg(2+) but there was no significant enhancement or inhibition of the activity with Ca(2+). However, other metal ions markedly inhibited its activity. Of all the natural vegetable oils tested, it had slightly higher hydrolytic activity on soybean oil compared to other oils. On TLC plate, the enzyme showed non-regioselective activity for triolein hydrolysis.