Nuanchawee Wetprasit

Quality assessment of noodles made from blends of rice flour and canna starch.

Canna starch and its derivatives (retrograded, retrograded debranched, and cross-linked) were evaluated for their suitability to be used as prebiotic sources in a rice noodle product. Twenty percent of the rice flour was replaced with these tested starches, and the noodles obtained were analyzed for morphology, cooking qualities, textural properties, and capability of producing short-chain fatty acids (SCFAs). Cross-linked canna starch could increase tensile strength and elongation of rice noodles. Total dietary fiber (TDF) content of noodles made from rice flour was 3.0% and increased to 5.1% and 7.3% when rice flour was replaced with retrograded and retrograded debranched starches, respectively. Cooking qualities and textural properties of noodles containing 20% retrograded debranched starch were mostly comparable, while the capability of producing SCFAs and butyric acid was superior to the control rice noodles; the cooked noodle strips also showed fewer tendencies to stick together.

Chebulin: Terminalia chebula Retz. fruit-derived peptide with angiotensin-I-converting enzyme inhibitory activity.

Angiotensin‐I–converting enzyme (ACE) plays an important role in blood pressure regulation. In this study, an ACE–hexapeptide inhibitor (Asp–Glu–Asn–Ser–Lys–Phe) designated as chebulin was produced from the fruit protein of Terminalia chebula Retz. by pepsin digestion, ultrafiltrated through a 3 KDa cut‐off membrane, a reverse‐phase high‐performance liquid chromatography, and nano‐liquid chromatography tandem mass spectrometry analysis. Chebulin was found to inhibit ACE in a noncompetitive manner, as supported by the structural model. It bounds to ACE by the hydrogen bond, hydrophobic and ionic interactions via the interactions of C‐terminal Phe (Phe‐6), and N‐terminal residues (Asp‐1 and Glu‐2) with the amino acid residues on noncatalytic sites of the ACE. The results showed that chebulin derived from fruits of T. chebula Retz. is a potential ACE–peptide inhibitor that could be used as a functional food additive for the prevention of hypertension and as an alternative to ACE inhibitor drug.

Bioactivities of Jc-SCRIP, a type 1 ribosome-inactivating protein from Jatropha curcas seed coat.

In this study, a type 1 RIP, designated as Jc‐SCRIP, was first isolated from the seed coat of Jatropha curcas Linn. It was purified by ammonium sulfate precipitation and chromatography on DEAE‐Sephacel™ and CM‐cellulose columns. Purification fold of Jc‐SCRIP increased 113.8 times, and the yield was 1.13% of the total protein in the final step. It was shown to be a monomeric glycoprotein with a molecular mass of 38 938 Da, as determined by MALDI‐TOF/MS. It exhibited hemagglutination activity and possessed strong N‐glycosidase activity. The antimicrobial activity of Jc‐SCRIP was tested against nine human pathogenic bacteria and one fungus; the most potent inhibitory activity was against Staphylococcus epidermidis ATCC 12228, with minimum inhibitory concentration value of 0.20 μm. Jc‐SCRIP demonstrated in vitro cytotoxicity against human breast adenocarcinoma cell line (MCF‐7), a colon adenocarcinoma (SW620), and a liver carcinoma cell line (HepG2), with IC50 values of 0.15, 0.25, and 0.40 mm, respectively. The results suggested that Jc‐SCRIP may be a potential natural antimicrobial and anticancer agent in medical applications.

Brucin, an antibacterial peptide derived from fruit protein of Fructus Bruceae, Brucea javanica (L.) Merr

A novel antibacterial peptide specific to Streptococcus pyogenes was produced from dried fruit protein of Brucea javanica (L.) Merr. A mixture of active peptides from the fruit protein was produced in vitro by pepsin hydrolysis. The hydrolysate was purified by reverse‐phase HPLC, and antimicrobial peptides active against Gram‐negative and Gram‐positive bacteria were analysed using SDS‐PAGE and nanoLC‐MS/MS. Here, four possible peptides were obtained and chemically synthesized for comparative study of the growth inhibition of Strep. pyogenes. One chemically synthesized peptide with a molecular mass of 1168·31 Da, His‐Thr‐Leu‐Cys‐Met‐Asp‐Gly‐Gly‐Ala‐Thr‐Tyr, showed the most potent antibacterial activity against Strep. pyogenes. This 11‐amino acid peptide was named Brucin. Its bacterial inhibitory activity was 16‐fold and 12·5‐fold higher than penicillin G and chloramphenicol, respectively, with a MIC value of 20 μmol l−1. The results suggest that Brucin, a potent antibiotic peptide, may be developed as an alternative drug for the treatment of the disease caused by Strep. pyogenes.

Antibacterial activities of crude extract from Punica granatum peels and its application

Methodology & Theoretical Orientation: To investigate an essential supply of oxygen, we studied our nanocapsules in a model of massive normovolemic hemodilution (NH) followed by an in vivo fluorescence microscopy analysis (IVM) to assess the microcirculation5. NH of 16 healthy wistar rats was performed stepwise below the critical hematocrit of a rat (10%) with nanocapsules and without ones (control), respectively. During NH systemic parameters (e.g. heart rate, mean arterial pressure (MAP), respiration, pH, pO2, lactate) were continuously monitored. At the end of NH rats were further observed up to 100 min and an IVM of the right leteral liver lobe was performed. Vessel diameters of sinusoids, post sinusoidal venules and the number of perfused sinusoidal vessels (%) were determined5.