Nonionic surfactants enhancing bactericidal activity at their critical micelle concentrations.

Bactericidal activities of benzalkonium chloride [also known as alkyldimethylbenzylammonium chloride (ADBAC)] containing nonionic surfactants such as methyl ester ethoxylates (MEE) with the alkyl group C8-C14 and oxyethylene (EO) group of average adduct number 3-15 were measured against Escherichia coli and Staphylococcus aureus. Sample solutions containing MEE in the vicinity of the critical micelle concentration exhibited a dramatic decrease in viable bacterial counts. MEE with an alkyl group of C12 and an oxyethylene group of lower adduct number exhibited little viable bacterial counts than those having higher EO adduct numbers. MEE with reduced EO adduct numbers increased fluorescence intensity in E. coli using the viability stain SYTO 9. Our results show that MEE molecules with low EO adduct numbers exhibited bactericidal activity by increasing the permeability of the E. coli cell membrane. Sample solution containing ADBAC and MEE molecules with lower EO adduct numbers also displayed higher zeta potentials. Moreover, ADBAC molecules incorporated into micelles of MEE with lower EO adduct numbers were adsorbed onto the surface of E. coli, which augmented bactericidal activity.

Virucidal effects of bleach activators, sodium alkyl acyloxybenzene sulfonate and acyloxybenzoic acid, against Feline calicivirus.

Noroviruses (NVs) are major causative pathogens of gastroenteritis. The disinfection of contaminated clothing during common household washing is desirable. The virucidal effects of 2 bleach activators, sodium alkyl acyloxybenzene sulfonate (OBS) and alkyl acyloxybenzoic acid (OBC), were studied using Feline calicivirus (FCV) as a surrogate for NVs. FCV was added to solutions containing either OBS or OBC and sodium percarbonate at various temperatures and for varying lengths of time. OBS and OBC, which generate long carbon chain peroxy acids, enhanced the virucidal effect of sodium percarbonate (PC). In particular, sodium lauroyloxybenzene sulfonate (OBS-12) and decanoyloxybenzoic acid (OBC-10) showed superior virucidal effects. Although the virucidal effect of 38-200 mg/L OBS-12 was maintained with 2-5% (v/v) horse serum, there was less of an effect with the same concentration of available chlorine. OBS and OBC have been used as ingredients in some laundry products to increase bleaching activity. It is expected that the use of OBS and OBC is also effective for the inactivation of NVs under common household washing conditions.

Effects of bleach activator, sodium alkyl acyloxybenzene sulfonate, on house dust mites (Dermatophagoides farinae).

House dust mites (Dermatophagoides farinae) in bedding and clothes are a major allergen. However, house dust mites cannot be killed by general washing conditions under 50 degrees C. Therefore, low-temperature washing conditions must be improved to eliminate house dust mites. Sodium alkyl acyloxybenzene sulfonate (OBS) is a bleach activator that is used to intensify the bleaching effects of some laundry products. The purpose of this study was to evaluate the effect of OBS on the elimination of house dust mites in low-temperature washing conditions. D. farinae was soaked in solutions containing different types of OBS for various durations and at various temperatures. The miticidal effects of the various washing conditions were also evaluated for D. farinae. Then sodium lauroyloxybenzene sulfonate (OBS-12) produced the highest D. farinae mortality rate among the OBS solutions that were examined and had a stronger miticidal effect than available chlorine under general washing conditions. OBS exhibited miticidal effects under general washing conditions at low temperatures. Since OBS is already used as an additive in some laundry products to increase the bleaching activity, OBS can be easily used to kill house dust mites under general washing conditions.

Allergen inactivation with colloidal silica.

We evaluated the allergen inactivating effect of colloidal silica by performing enzyme-liked immunosorbent assay (ELISA) whose wells were coated with 150 ng/mL of Japanese cedar pollen allergen (Cry j 1) or mite allergen (Der f 2). The allergens were almost 100% inactivated by 100 microg/mL of colloidal silica having a particle size 5 nm, and the inactivating effect was increased by aluminum binding to the surface of the colloidal silica. The results show that colloidal silica is a promising material for allergen inactivation. Since colloidal silica forms an insoluble nondispersive solid when dried, it is expected that airborne allergens can be reduced by binding them to colloidal silica.

Expression of Bacillus protease (Protease BYA) from Bacillus sp. Y in Bacillus subtilis and enhancement of its specific activity by site-directed mutagenesis-improvement in productivity of detergent enzyme-.

An attempt was made to express protease BYA produced by an alkalophilic Bacillus sp. Y in Bacillus subtilis by gene engineering methods. The gene encoding protease BYA was cloned from Bacillus sp. Y, and expression vector pTA71 was constructed from the amylase promoter of Bacillus licheniformis, DNA fragments encoding the open reading frame of protease BYA, and pUB110. Protease BYA was secreted at an activity level of 5100 APU/ml in the common industrial culture medium of Bacillus subtilis transformed with pTA71. We then attempted to increase the specific activity of protease BYA by site-directed mutagenesis. Amino acid residue Ala29 next to catalytic Asp30 was replaced by one of three uncharged amino acid residues (Val29, Leu29, Ile29), and each mutant enzyme was expressed and isolated from the culture medium. Val29 mutant enzyme was secreted at an activity level of greater than 7000 APU/ml in culture medium, and its specific activity was 1.5-fold higher than that of the wild-type enzyme. Other mutant enzymes had specific activity similar to that of the original one and were less stabile than the wild-type enzyme. It can be thought that the substitution at amino acid residue 29 affects the level of activity and stability of protease BYA.