Removal of tetramethylammonium hydroxide (TMAH) by cold plasma treatment combined with periodate oxidation: Degradation, kinetics, and toxicity study.

Tetramethylammonium hydroxide (TMAH), which is a chemical used in the electronic industry, is classified as a hazardous material (HAZMAT class 8) that threatens aquatic ecosystems and human health. Consequently, numerous studies have attempted to remove TMAH using various treatment methods, including advanced oxidation processes such as ozone, UV, or Fenton oxidation. However, prior research has indicated a low kinetic rate of TMAH removal. In this context, we proposed an alternative to TMAH degradation by combining a cold plasma (CP) process with periodate oxidation. As for the kinetics of TMAH removal, the kinetic constant was improved by 5 times (0.1661 and 0.0301 for 40.56 and 2.2 W, respectively) as the electric power of a CP system increased from 2.2 to 40.56 W. The kinetic constant of a 40.56 W CP system further increased by 54 times (1.6250) than a 2 W CP system when 4 mM periodate was used simultaneously. As a result, the integrated CP/periodate system represented 2 times higher TMAH removal efficiency (29.5%) than a 2 W CP system (14.4%). This excellent TMAH degradation capability of the integrated CP/periodate system became pronounced at pH 10 and 25 °C. Overall, the integrated CP/periodate system is expected to be a viable management option for effectively controlling hazardous TMAH chemicals.

Effects of cold plasma pretreatment combined with sodium periodate on property enhancement of dialdehyde starch prepared using native maize starch.

This study represents the inaugural investigation into the effect of cold plasma (CP) pretreatment combined with sodium periodate on the preparation of dialdehyde starch (DAS) from native maize starch and its consequent effects on the properties of DAS. The findings indicate that the maize starch underwent etching by the plasma, leading to an increase in the particle size of the starch, which in turn weakened the rigid structure of the starch and reduced its crystallinity. Concurrently, the plasma treatment induced cleavage of the starch molecular chain, resulting in a decrease in the viscosity of the starch and an enhancement of its fluidity. These alterations facilitated an increased contact area between the starch and the oxidising agent sodium periodate, thereby augmenting the efficiency of the DAS preparation reaction. Consequently, the aldehyde group content was elevated by 9.98 % compared to the conventional DAS preparation methodology. Therefore, CP could be an efficient and environmentally friendly non-thermal processing method to assist starch oxidation for DAS preparation and property enhancement.

Periodate oxidation of nanofibrillated cellulose films for active packaging applications.

An alternative packaging material based on cellulose that possesses excellent barrier properties and is potentially useful for active packaging has been developed. Cellulose nanofibril was efficiently and selectively oxidized with sodium periodate generating reactive aldehyde groups. These groups formed hemiacetal and hemialdal bonds during film formation and, consequently, highly transparent, elastic and strong films were created even under moisture saturation conditions. The periodate oxidation treatment additionally decreased the polarity of the films and considerably enhanced their water barrier properties. Thus, the water contact angle of films treated for 3 and 6 h was 97° and 102°, their water drop test value was higher than in untreated film (viz., 138 and 141 min with 3 and 6 h of treatment) and their water vapour transmission rate was substantially better (3.31 and 0.78 g m-2 day-1 with 3 and 6 h, respectively). The presence of aldehyde groups facilitated immobilization of the enzyme laccase, which efficiently captures oxygen and prevents food decay as a result. Laccase-containing films oxidized 80 % of Methylene Blue colorant and retained their enzymatic activity after storage for 1 month and 12 reuse cycles, opening the door to the possible creation of a reusable packaging to replace the single-use packaging.

Characterization and bioactivities of a novel polysaccharide obtained from Gracilariopsis lemaneiformis

ABSTRACT Gracilariopsis lemaneiformis is a type of red alga that contains seaweed polysaccharide agar. In this study, a novel non-agar seaweed polysaccharide fraction named GCP (short of crude polysaccharide obtained from Gracilariopsis lemaneiformis) was isolated from Gracilariopsis lemaneiformis. Structural analysis showed that GCP shows triple helical chain conformation when dissolved in water and has many branches and long side chains. Also, 1→3 linkage is the major linkage and the sugar structures are galactopyranose configurations linked by β-type glycosidic linkages. Two macromolecular substance fractions (GCP-1 and GCP-2) were purified by DEAE Sepharose Fast Flow column chromatography. Moreover, a splenocyte damage assay and splenocyte proliferation assay were used to analyse the bioactivities of GCP, GCP-1 and GCP-2. It was demonstrated that polysaccharides could protect splenocyte damaged by H2O2; GCP-2 shows a greatest protection rate, that is, 92.8%, which significantly enhanced the splenocyte proliferation, and GCP showed the highest proliferation rate, 9.30%. The results suggested that this type of novel non-agar polysaccharide displayed remarkable antioxidant and immunomodulatory activities and early alkali treatment could decrease the activities. It may represent a potential material for health food and clinical medicines.

Enzymatic N-glycan analysis of 31 kDa molecule in plerocercoid of Spirometra mansoni (sparganum) and its antigenicity after chemical oxidation

A highly specific antigenic protein of 31 kDa from plerocercoid of Spirometra mansoni (sparganum) was obtained by gelatin affinity and Mono Q anion-exchange column chromatography. The purified 31 kDa protein was subjected to N-glycan enzymatic digestion for structural analysis. The relative electrophoretic mobility was analyzed by SDS-PAGE, before and after digestion. On SDS-PAGE after enzymatic digestion, the 31 kDa protein showed a molecular shift of approximately 2 kDa, which indicated the possession of complex N-linked oligosaccharides (N-glycosidase F sensitive) but not of high-mannose oligosaccharides (endo-beta-N-acetylglucosaminidase H, non-sensitive). Chemically periodated 31 kDa protein showed statistically non-significant changes with human sparganosis sera by enzyme linked immunosorbent assay (ELISA). Therefore, the dominant epitopes of the 31 kDa molecule in human sparganosis were found to be mainly polypeptide, while N-glycans of the antigenic molecule in sparganum was minimal in anti-carbohydrate antibody production.