Pyrolysis of Cellulose

Comparative study of acetaldehyde, furfural and 5-hydroxymethyl furfural from celluloses which differed in crystallinity was made by pyrolytic gas chromatography.

Pyrolysis of tobacco cellulose at 200~300°C resulted in rapid increase in the yields of furfurals from the amorphous regions in comparison with that from the crystalline regions. At 500°C, however, acetaldehyde was obtained in higher yields from microcrystalline cellulose than that from tobacco cellulose under the same condition.

In thermogravimetric analysis, the threshold temperature for the pyrolysis of tobacco cellulose was lower than that of microcrystylline cellulose. These results showed that the yields of the volatile compounds from pyrolysis of cellulose depended on temperature and crystallinity.     

Metabolic Fate of O-Ethyl S,S-Diphenyl Phosphorodithiolate (Hinosan®) in Rice Plant

Metabolism and residual fate of O-ethyl S,S-diphenyl phosphorodithiolate (Hinosan®) applied on rice plant was examined by using ³⁵S-labeled or ³²P-labeled compound. Ion exchange chromatography, thin-layer chromatography and gas-liquid chromatography with flame thermionic detector or flame photometric detector were applied for identification of water soluble and toluene soluble metabolites of Hinosan. Degradation of Hinosan at the initial stage of metabolism was mainly the cleavage of P-S linkage, and a large portion of phenyl dihydrogen phosphorothiolate and a minor portion of O-ethyl S-phenyl hydrogen phosphorothiolate were found as water soluble metabolites. Phenylthio radical released on the production of the above mentioned metabolites was recovered as diphenyl disulfide, which was finally converted to sulfuric acid through benzenesulfonic acid. Triphenyl phosphorotrithiolate and O,O-diethyl S-phenyl phosphorothiolate were produced by transesterification between molecules of Hinosan at the initial stage of metabolism. Examination of metabolites in rice grains showed that sulfur and phosphorus atoms in Hinosan were incorporated into neutral or cationic substances probably after several steps of chemical transformation.     

Effet d'anesthesiques locaux sur le transfert de mannose dans les membranes microsomiques d'Aspergillus niger van Tieghem

The influence of various local anaesthetics has been studied on the mannose transfer enzymic system which is localized in Aspergillus niger van Tieghem microsomal membranes. The n-alcanes and tertiary amines do not seem to react on the first step of the reaction: i.e. the polyprenylphosphate-mannose biosynthesis. However two amines, the dibucaine and to a lesser extent the tetracaine, inhibit the mannose transfer from the polyprenylphosphate-mannose to the endogenous proteins.     

Regulation of larval diapause by juvenile hormone in the European corn borer,Ostrinia nubilalis

The effects of juvenile hormone (JH) on the larval diapause of the European corn borer, Ostrinia nubilalis, were investigated. The larval period was prolonged and the development of gonads was retarded if non-diapause larvae were treated with JH. Pupation of diapausing larvae was accelerated by allatectomy. It was concluded that the diapause of this borer is largely regulated by JH.     

Electrostatic role of aromatic ring stacking in the pH-sensitive modulation of a chymotrypsin-type serine protease, Achromobacter protease I.

Achromobacter protease I (API) has a unique region of aromatic ring stacking with Trp169-His210 in close proximity to the catalytic triad. This paper reveals the electrostatic role of aromatic stacking in the shift in optimum pH to the alkaline region, which is the highest pH range (8.5-10) among chymotrypsin-type serine proteases. The pH-activity profile of API showed a sigmoidal distribution that appears at pH 8-10, with a shoulder at pH 6-8. Variants with smaller amino acid residues substituted for Trp169 had lower pH optima on the acidic side by 0-0.9 units. On the other hand, replacement of His210 by Ala or Ser lowered the acidic rim by 1.9 pH units, which is essentially identical to that of chymotrypsin and trypsin. Energy minimization for the mutant structures suggested that the side-chain of Trp169 stacked with His210 was responsible for isolation of the electrostatic interaction between His210 and the catalytic Asp113 from solvent. The aromatic stacking regulates the low activity at neutral pH and the high activity at alkaline pH due to the interference of the hydrogen bonded network in the catalytic triad residues.