Effect of a probiotic Lactobacillus plantarum TN8 strain on trinitrobenzene sulphonic acid‐induced colitis in rats

This study aimed to investigate the potential effects of an oral treatment by a newly isolated probiotic Lactobacillus plantarum TN8 strain on trinitrobenzene sulphonic acid (TNBS)‐induced colitis in Wistar rats. Thus, 18 rats were divided into three groups (n = 6 per group): group 1 (control) – rats not receiving TNBS application; group 2 – rats receiving an intrarectal TNBS infusion (100 mg/kg TNBS dissolved in ethanol); and group 3 – rats treated with intragastrical TN8 strain once per day (for 5 days before TNBS induction). The performance and the effects of the probiotic treatment were evaluated using a series of histological, biophysical and biochemical analyses. The results have shown that the treatment with the L. plantarum TN8 strain improves the body weight and reduces the diarrhoea, colonic mucosal inflammation and colon shortening. TN8‐treated rats showed a significant decrease in the total cholesterol content from 1.86 (for group 2) to 1.32 mmol/l and in triglyceride (TG) content from 2.09 (for group 2) to 1.23 mmol/l. Furthermore, the findings revealed that the high‐density lipoprotein (HDL) cholesterol contents increased from 0.95 to 1.02 mmol/l. The histological studies have confirmed that the architecture of the liver and kidney tissues of the TN8‐treated rats were found to be improved. Overall, the results suggest that the L. plantarum TN8 presents promising perspectives for the development of safe and cost‐effective agents for the prevention or alleviation of several intestinal pathologies.     

Effect of Degree of Hydrolysis and Protease Type on the Antioxidant Activity of Protein Hydrolysates From Cuttlefish (Sepia officinalis) By-Products

We have investigated the antioxidant activities of eight hydrolysates from cuttlefish by-products obtained by treatment with various gastrointestinal proteases (chymotrypsin, trypsin, and crude alkaline enzyme extracts from cuttlefish and sardinelle) and bacterial proteases (Alcalase and crude enzymes from Bacillus pumilus A1, Bacillus mojavensis A21, and Bacillus cereus BG1). The antioxidant activities of the cuttlefish by-products protein hydrolysates (CPHs) were evaluated using various in vitro antioxidant assays, such as 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical-scavenging activity, reducing power, and total antioxidant capacity. All hydrolysates showed different degrees of hydrolysis (DH) and varying degrees of antioxidant activity. Among the different hydrolysates, cuttlefish crude enzyme hydrolysate exhibited the highest antioxidant activity, followed by sardinelle crude enzyme and Alcalase hydrolysates. Further, CPHs with different degrees of hydrolysis were prepared by treatment with proteolytic enzymes from cuttlefish, sardinelle, and B. mojavensis A21. All hydrolysates showed a greater antioxidative activity as indicated by all the methods considered. In addition, antioxidant activity in hydrolysates was positively correlated with the increase of DH. The results of this study indicated that CPHs might be a good candidate for further investigation in developing new antioxidants.     

Golden Grey Mullet (Liza aurata) Alkaline Proteases: Biochemical Characterization,Application in the Shrimp Wastes Deproteinization,Laundry Commercial Detergents,and Preparation of Antioxidant Protein Hydrolysate

Digestive alkaline proteinases from golden grey mullet (Liza aurata) were extracted and characterized. The crude alkaline protease showed optimum activity at pH 8.0 and 60°C, and it was highly stable over a wide range of pH from 4.0 to 10.0, retaining more than 80% activity after incubation for 1 h at 4°C. The alkaline proteases showed extreme stability toward nonionic and anionic surfactants after preincubation for 1 h at 25°C and relative stability toward oxidizing agents. Additionally, the crude enzyme showed excellent stability and compatibility with various solid and liquid detergents. Further, proteases from golden grey mullet viscera were found to be effective in the deproteinization of shrimp wastes. The protein removal after 3 h at 45°C with an enzyme/substrate (E/S) ratio of 10 U/mg protein was about 76%. The golden grey mullet proteases were also shown to be efficient in the production of antioxidant protein hydrolysate.     

Isolation and Characteristics of Carboxypeptidase B from Zebra Blenny (Salaria basilisca) Viscera

Carboxypeptidase B (CPB) from zebra blenny (Salaria basilisca) viscera was purified using ammonium sulphate precipitation and Sephadex G-100 gel filtration, with a 28-fold increase in specific activity and 21.72% recovery. The molecular weight of the enzyme was estimated to be 34.5 kDa by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). The optimum pH and temperature for the enzyme activity were around pH 8.0 and 60°C, respectively, using Hippuryl-l-Arg as a substrate. The enzyme was unstable above 50°C and below pH 5.0. The enzyme was activated by Co²⁺ and Zn²⁺ and inhibited by ethylenediaminetetraacetic acid (EDTA). The N-terminal amino acid sequence of the enzyme was determined as S P S Y T K Y N T. The CPB kinetic constants, K_m and k_cat for Hippuryl-l-Arg, were 0.32 mM and 36.23 s^?1, respectively.