Sodium Cardanol Sulfonate Surfactant from Cashew Nut Shell Liquid

Sodium cardanol sulfonate surfactant was synthesized from cardanol from cashew nut shell liquid. Surfactant properties of cardanol sulfonate were determined and compared with dodecylbenzene sulfonate. Surface tension values were determined to be 32.25 mN/m for cardanol sulfonate at 20% w/v and 28.00 mN/m for dodecylbenzene sulfonate at 15% w/v. Critical micelle concentrations of dodecylbenzene sulfonate and cardanol sulfonate were found to be 0.435 and 0.372 mol/L, respectively. In comparison with dodecylbenzene sulfonate, the relative detergency of cardanol sulfonate was calculated to be 93.7% compared to dodecylbenzene sulfonate. Results suggest that cardanol sulfonate can be used as alternative anionic surfactant.

Development of fermented Hericium erinaceus juice with high content of L‐glutamine and L‐glutamic acid

Fermented plant beverages (FPB) with a high content of desirable principle components are served as functional foods from several years. Hericium erinaceus is famous for its antimicrobial, antioxidant, antihypertensive and antidiabetic nature. Accordingly, the current study was aimed to produce fermented H. erinaceus juice with a high content of L‐glutamine (Gln) and L‐glutamic acid (GA) through lactic acid bacteria (LAB) isolated from fermented Thai foods. LAB isolates were screened and identified the potent protease‐producing bacteria Enterococcus faecalis (G414/1) that facilitate the production of Gln and GA through protein hydrolysis. Box–Behnken design (BBD) and response surface methodology (RSM) were adapted for the optimisation of conditions for the increased production of Gln and GA during fermentation of H. erinaceus. We succeeded with an optimum concentration of cofactor (CaCl₂), pH and temperature for improved protease activity and subsequent Gln and GA production. The ability of isolated E. faecalis strain to produce Gln and GA was demonstrated in this study. Further, upstream processes like strain improvement and media optimisation will direct the way to produce enriched H. erinaceus based FPB.     

Toxicity of anionic detergents determined by Saccharomyces cerevisiae microarray analysis

Sodium n-dodecyl benzene sulfonate (LAS) and sodium dodecyl sulfate (SDS) are popular anionic detergents (surfactants) that are used worldwide and the toxicities of these chemicals have been characterized. We applied these chemicals in a DNA microarray bioassay and determined that the microarray data reflects previous findings and also provides some new information about anionic detergent toxicity. The mRNA expression profiles suggest that LAS and SDS cause damage to membranes and alterations in carbon metabolism, and induce the oxidative stress response. We also found that LAS and SDS induce the pleiotropic drug-resistance network, and that LAS and SDS may be pumped out of yeast cells by this network. Hierarchical clustering of the expression profiles showed that LAS and SDS cause similar features of toxicity and that the toxicity is similar to that of capsaicin but different from that of cadmium and mercury.     

Bifidobacterial GH146 β-l-Arabinofuranosidase (Bll4HypBA1) as the Last Enzyme for the Complete Removal of Oligoarabinofuranosides from Hydroxyproline-Rich Glycoproteins

In plant cell walls, the hydroxyproline-rich glycoproteins (HRGPs) such as extensin contain oligoarabinofuranoside linked to a hydroxyproline (Hyp) residue. The mature arabinooligosaccharide was revealed to be a tetrasaccharide (α-l -Araf-(1→3)-β-l -Araf-(1→2)-β-l -Araf-(1→2)-β-l -Araf, l -Araf₄), whose linkages are targets of the bifidobacterial and Xanthomonas arabinooligosaccharide-degrading enzymes. The l -Araf₄ motif was cleaved by GH43 α-l -arabinofuranosidase (Arafase) and converted to an l -Araf₃-linked structure. The latter is then cleaved by GH121 β-l -arabinobiosidase (HypBA2), producing β-l -Araf-(1→2)-l -Ara (β-l -arabinobiose) and mono-β-l -Araf linked to the HRGP backbone. In bifidobacteria, the β-l -arabinobiose is then hydrolyzed by GH127 β-l -Arafase (Bll1HypBA1), a mechanistically unique cysteine glycosidase. We recently identified the distantly related homologue from Xanthomonas euvesicatoria as GH146 β-l -Arafase along with paralogues from Bifidobacterium longum, one of which, Bll4HypBA1 (BLLJ_0089), can degrade l -Araf₁-Hyp in a similar way to that of GH146. As the chemical synthesis of the extensin hydrophilic motif 1 a , which possesses three distinct linkages that connect four oligoAraf residues [Hyp(l -Araf_n) (n=4, 3, 1)], was achieved previously, we precisely monitored the step-wise enzymatic cleavage of 1 a in addition to that of potato lectin. The results unequivocally revealed that this enzyme specifically degrades the Hyp(l -Araf₁) motif.     

Hemagglutinating activity and corresponding putative sequence identity from Curcuma aromatica rhizome

BACKGROUND: Curcuma aromatica is a medicinal plant belonging to the Zingiberaceae family with an incomplete genome sequence. It has been reported that extract from the rhizome of this plant contains haemagglutinating activity. In this study the profile of fractions containing hemagglutinating activity is described. RESULTS: Following extraction with saline buffer, the protein solution was fractionated by ammonium sulfate precipitation. Ion‐exchange chromatography was completed on fast‐flow SP‐Sepharose, as well as gel filtration chromatography on Superdex 75. The active fractions were then separated by one‐dimensional sodium dodecyl sulfate–polyacrylamide gel electrophoresis and labeled proteins were digested with trypsin. The digest bands were analyzed by reversed‐phase liquid chromatography—tandem mass spectrometry. Inferred peptide sequences were used in Mascot searching and mass spectrometry‐driven BLAST (MS‐BLAST) homology searches allowed the recognition of related proteins in other species of Viridiplantae. Six putative proteins from nine bands showed similarity with lectin sequences. CONCLUSION: This study reports the identification of six lectins from the Curcuma aromatica rhizome achieved by mass spectrometry using MS‐BLAST algorithms to search for homology between de novo determined peptide sequences and protein sequences available in sequence databases. Copyright © 2008 Society of Chemical Industry     

Brominated phenol–formaldehyde resin as an adhesive for plywood

A brominated phenol–formaldehyde resin was investigated as a plywood adhesive to study the effect of bromine on the physical and flammability properties of this resin. The results of these studies showed that brominated phenol–formaldehyde resin of 10% bromine content by weight of the phenol–formaldehyde resin was suitable to be used as a plywood adhesive. The optimal compressing temperature and compressing time were 110°C and 30 min, respectively. The prepared plywood obtained from the optimal condition gave a high shear strength, good flame retardancy, and good resistance to both hot and cold water. © 2003 Wiley Periodicals, Inc. J Appl Polym Sci 89: 1918–1924, 2003