Antifungal activity and enhancement of plant growth by Bacillus cereus grown on shellfish chitin wastes.

Bacillus cereus QQ308 produced antifungal hydrolytic enzymes, comprising chitinase, chitosanase and protease, when grown in a medium containing shrimp and crab shell powder (SCSP) produced from marine waste. The growth of the plant-pathogenic fungi Fusarium oxysporum, Fusarium solani, and Pythium ultimum were considerably affected by the presence of the QQ308 culture supernatant. The supernatant inhibited spore germination and germ tube elongation of F. oxysporum, F. solani, and P. ultimum. The increase in the growth time of the fungal culture was associated with a gradual decrease in inhibition. Besides antifungal activity, QQ308 enhanced growth of Chinese cabbage. These characteristics were unique among known strains of B. cereus. To our knowledge, this is the first report on the antifungal and Chinese cabbage growth enhancing compounds produced by B. cereus.

A study to evaluate the potential of an in silico approach for predicting dipeptidyl peptidase-IV inhibitory activity in vitro of protein hydrolysates.

A total of 294 edible protein sequences and 5 commercial proteases listed in the BIOPEP database were analyzed in silico. The frequency (A), a parameter in silico described previously, was examined further to calculating the ratio of truncated peptides with Xaa-proline and/or Xaa-alanine to all peptide fragments in a protein hydrolyzed with a protease, using the BIOPEP database. Then the in vitro DPP-IV inhibitory activity was determined using the same 15 protein and protease combinations to evaluate their relationship. The result shows that A values considering the number of Xaa-proline+Xaa-alanine exhibited a strong correlation with in vitro DPP-IV inhibition rates by Pearson's correlation analysis (r=0.6993; P<0.05). Therefore, the in silico approach is effective to predict DPP-IV inhibitory activities in vitro of protein hydrolysates.

In silico, in vitro and in vivo analyses of dipeptidyl peptidase IV inhibitory activity and the antidiabetic effect of sodium caseinate hydrolysate.

The frequency (A), a novel in silico parameter, was developed by calculating the ratio of the number of truncated peptides with Xaa-proline and Xaa-alanine to all peptide fragments from a protein hydrolyzed with a specific protease. The highest in vitro DPP-IV inhibitory activity (72.7%) was observed in the hydrolysate of sodium caseinate by bromelain (Cas/BRO), and the constituent proteins of bovine casein also had relatively high A values (0.10-0.17) with BRO hydrolysis. 1CBR (the <1 kDa fraction of Cas/BRO) showed the greatest in vitro DPP-IV inhibitory activity of 77.5% and was used for in vivo test by high-fat diet-fed and low-dose streptozotocin-induced diabetic rats. The daily administration of 1CBR for 6 weeks was effective to improve glycaemic control in diabetic rats. The results indicate that the novel in silico method has the potential as a screening tool to predict dietary proteins to generate DPP-IV inhibitory and antidiabetic peptides.

The development of bioactive peptides from dietary proteins as a dipeptidyl peptidase IV inhibitor for the management of type 2 diabetes.

One of the new approaches to the management of type 2 diabetes mellitus (T2DM) consists of orally administered dipeptidyl peptidase-IV (DPP-IV) inhibitors. These synthetic drug inhibitors are reported to have some side effects and that subsequently limits their applications. There is a growing interest to develop natural DPP-IV inhibitors that will be potent without undesirable side effects. Many in vitro and some in vivo studies have highlighted the potential of food-derived peptides functioning as effective DPPIV inhibitors. Bioactive peptides within original food-derived proteins are inactive but can be activated by being released during food processing (by enzymatic hydrolysis or fermentation) or during gastrointestinal digestion. Hence, the utilization of computer-aided techniques as screening tools may be helpful in predicting the potential of food proteins as precursors of DPP-IV inhibitory peptides. This paper reviews the current literature on DPP-IV inhibitory peptides, focusing on their in vitro activity and in vivo antidiabetic effects. In addition, the feasibility of various in silico approaches is also summarized in this review.

Dipeptidyl-peptidase IV inhibitory activity of peptides derived from tuna cooking juice hydrolysates.

The in vitro DPP-IV inhibitory activity of isolated peptides from of tuna cooking juice hydrolyzed by Protease XXIII (PR) and orientase (OR) was determined. The results showed that the peptide fractions with the molecular weight over 1,422 Da possessed the greatest DPP-IV inhibitory activity. The amino acid sequences of the three peptides isolated from PR and OR hydrolysates were identified by MALDI-TOF/TOF MS/MS, and they were Pro-Gly-Val-Gly-Gly-Pro-Leu-Gly-Pro-Ile-Gly-Pro-Cys-Tyr-Glu (1412.7 Da), Cys-Ala-Tyr-Gln-Trp-Gln-Arg-Pro-Val-Asp-Arg-Ile-Arg (1690.8 Da) and Pro-Ala-Cys-Gly-Gly-Phe-Try-Ile-Ser-Gly-Arg-Pro-Gly (1304.6 Da), while they showed the dose-dependent inhibition effect of DPP-IV with IC(50) values of 116.1, 78.0 and 96.4 µM, respectively. In vitro simulated gastrointestinal digestion retained or even improved the DPP-IV inhibitory activities of the three peptides. The results suggest that tuna cooking juice would be a good precursor of DPP-IV inhibitor, and the DPP-IV inhibitory peptides can successfully passed through the digestive tract.

Peptides derived from atlantic salmon skin gelatin as dipeptidyl-peptidase IV inhibitors.

The dipeptidyl-peptidase IV (DPP-IV)-inhibitory activity of peptides derived from Atlantic salmon skin gelatin hydrolyzed by alcalase (ALA), bromelain (BRO), and Flavourzyme (FLA) was determined. The FLA hydrolysate with the enzyme/substrate ratio of 6% showed the greatest DPP-IV-inhibitory activity. The hydrolysate was fractionated by ultrafiltration with 1 and 2.5 kDa cutoff membranes, and the <1 kDa fraction had the highest DPP-IV-inhibitory activity with an IC(50) value of 1.35 mg/mL. The F-1 fraction further isolated by HPLC showed the IC(50) value against DPP-IV of 57.3 µg/mL, and the peptide sequences were identified as Gly-Pro-Ala-Glu (372.4 Da) and Gly-Pro-Gly-Ala (300.4 Da). The synthetic peptides showed dose-dependent inhibition effects on DPP-IV with IC(50) values of 49.6 and 41.9 µM, respectively. The results suggest that the peptides derived from Atlantic salmon skin gelatin would be beneficial ingredients for functional foods or pharmaceuticals against type 2 diabetes.

Effects of hydrostatic pressure/heat combinations on water uptake and gelatinization characteristics of japonica rice grains: a kinetic study.

The combination effects of pressure (200 to 500 MPa) and temperature (20, 40, and 50 degrees C) on the water uptake and gelatinization characteristics of japonica rice (Tainung 71) grains were investigated. Pressure greater than 200 MPa at all temperatures increased the moisture content and volume of rice grains; meanwhile, the increase content of rice grain volume showed a high correlation with that of moisture content (r(2)= 0.96). The highest degree of gelatinization of 73% was observed at 500 MPa and 50 degrees C for 120 min, while gelatinization did not occur at pressures below 300 MPa and temperatures of 20 and 40 degrees C. The rate of gelatinization followed the 1st-order kinetics at each temperature and pressure. The higher pressures and temperatures would result in higher values of rate constant k which could be correlated with both pressure and temperature by combining Arrhenius and Eyring models.