Hydrolytic degradation of poly(oxyethylene)–poly-(ε-caprolactone) multiblock copolymers

The degradation of poly(oxyethylene)–poly(ε-caprolactone) (POE–PCL) multiblock copolymers was investigated at 37°C in a 0.13M, pH 7.4 phosphate buffer selected to mimic in vivo conditions. The copolymers were obtained by coupling polycaprolactone diols and poly(ethylene glycol) diacids using dicyclohexylcarbodiimide as coupling agent. Various techniques, such as weighing, size exclusion chromatography, infrared, ¹H nuclear magnetic resonance, differential scanning calorimetry, and X-ray diffractometry, were used to monitor changes in total mass, water absorption, molar mass, thermal properties, degree of crystallinity, and composition. The results showed that introduction of POE sequences considerably increased the hydrophilicity of the copolymers as compared with PCL homopolymers. Nevertheless, the degradability of PCL sequences was not enhanced due to the phase separation between the two components. Significant morphological changes were also observed during the degradation. © 1998 John Wiley & Sons, Inc. J Appl Polym Sci 68: 989–998, 1998     

Investigation of alkaline hydrolysis of polyethylene terephthalate by differential scanning calorimetry and thermogravimetric analysis

The hydrolytic depolymerization of polyethylene terephthalate (PET) with alkaline hydroxides was investigated by differential scanning calorimetry (DSC) and thermogravimetric analysis (TGA). The reactions of the mixtures were conducted in their solid states under nitrogen atmosphere. The experimental results showed that potassium hydroxide possessed the hydrolytic activity of depolymerizing PET into small molecules such as ethylene glycol; in contrast, sodium hydroxide did not. The production rate of ethylene glycol was enhanced by increasing charge ratio of potassium hydroxide to PET. The presence of water facilitated the alkaline hydrolysis of PET; however, the presence of metal acetates decreased the hydrolysis rate. The activation energy for alkaline hydrolysis of PET determined by the thermograms was in good agreement with the value obtained from the experiments in a batch reactor. © 1998 John Wiley & Sons, Inc. J Appl Polym Sci 70: 1939–1945, 1998     

Differential hydrolysis of alk(en)yl cysteine sulphoxides by alliinase in onion macerates: flavour implications

Intact cells of Allium spp have no odour, but when cells are disrupted, the enzyme alliinase (EC 4.4.1.4) hydrolyses the S-alk(en)yl sulphoxides (ACSOs) to produce pyruvate, ammonia and the many volatile sulphur compounds associated with flavour and odour. In onions, there are three main sulphoxides: methyl, propyl and 1-propenyl, which gives rise to onion's tear-producing effect. The relative proportions of these are a factor in determining the subsequent flavour. γ-Glutamyl peptides, which are biosynthetic intermediates to ACSOs, are also present in significant amounts, but their contribution to flavour is not known. There is little work on the reaction of alliinase in vivo. The hydrolysis of ACSOs by alliinase was studied in rapidly macerated bulbs at intervals between 5 s and 2 h. ACSO and γ-glutamyl peptide levels were measured by HPLC, and pyruvate levels were measured spectrophotometrically. Although the hydrolysis of propenyl cysteine sulphoxide (PrenCSO) was immediate and almost 100% between 5 and 20 s after bulb maceration, the hydrolysis of propyl cysteine sulphoxide (PCSO) and methyl cysteine sulphoxide (MCSO) was incomplete. After 5 s maceration, about 50% PCSO and MCSO remained and thereafter no further hydrolysis occurred. The levels of ACSOs and the extent to which they were hydrolysed were dependent on the cultivar and sulphur environment in which it was grown. The addition of pyridoxal phosphate cofactor enhanced the extent of MCSO and PCSO hydrolysis. Additional purified alliinase per se had no effect. Substantial hydrolysis of γ-glutamyl peptides also occurred after maceration, and this was unexpected. Levels of pyruvate product were between 15 and 25% of the expected amount from ACSO hydrolysis assuming a stoichiometric relationship. The incomplete hydrolysis of MCSO and PCSO, enhancement of activity by additional pyridoxal phosphate and non-stoichiometric production of pyruvate are evidenced that reaction inhibition of alliinase may be occurring in onion macerates. © 1998 Society of Chemical Industry.     

纤维素/半纤维素酶配合漆酶预处理马尾松未漂磨石磨木浆的研究

分别用半纤维素酶PulpzymeHC、纤维素酶Novozym476对马尾松未漂磨石磨木浆(GP)进行预处理,然后再进行NS51003漆酶/介体系统生物酶处理及后续的H2O2漂白,并对酶处理浆在H2O2漂白前后白度和强度性能进行测定。研究结果表明,利用半纤维素酶PulpzymeHC、纤维素酶Novozym476对马尾松未漂磨石磨木浆(GP)进行预处理,可有效提高漆酶NS51003处理马尾松未漂GP的效率,更加有效的提高纸浆的白度及强度性能,而且适当的预处理可使纸浆具有更好的可漂性,从而使H2O2漂白后的酶处理浆具有更高的白度和更好的强度性能。     

Impact of bioethanol impurities on steam reforming for hydrogen production: A review

Hydrogen fuel cells (H₂–FCs) are promising devices for pollution-free and efficient power production. Renewable H₂ from biomass is often produced through catalytic ethanol steam reforming (ESR), which requires a steam/ethanol molar ratio of at least three. The bioethanol obtained by biomass fermentation contains large amounts of water and can be directly subjected to ESR without complex purification steps. However, a wide spectrum of impurities is present in such bioethanol samples, thus complicating the ESR process. Acetic acid, fusel alcohols, ethyl acetate, and sulfur components have been reported as important bioethanol impurities, and also as the main precursors of carbon deposits on the ESR catalyst. On the other hand, amines, methanol, and aldehydes, which are minor bioethanol impurities, have been reported to enhance the H₂ production. This review seeks to define alternatives to reduce the above negative impurities and increase the positive ones during biomass pretreatment and fermentation. Additionally, ESR catalysts are reviewed to identify the features that make them more resistant to deactivation. The combination of strategies to control the impurities during biomass pretreatment, fermentation, purification and the development of highly resistant catalysts may allow processes to produce H₂ from biomass with a low carbon footprint, rendering H₂–FCs an environmentally friendly technology for power production.     

硫化物生物浸出过程中木质纤维素的应用现状

生物浸出技术具有成本低、无污染、要求简单的特点,已被成功应用于很多金属硫化矿物的回收。但生物浸出速度慢、浸出率低的问题一直存在,特别是黄铜矿。木质纤维素作为一种廉价的可再生资源,可以加速生物浸出过程,比如废旧报纸、稻壳、竹屑等。对木质纤维素在生物浸出中的应用研究进行回顾,讨论木质纤维素的硫酸水解问题,对比分析添加木质纤维素对生物浸出效率、矿物、ORP、pH、Fe3+/Fe2+、微生物群落等的综合影响。总结了木质纤维素促进生物浸出的机理,并讨论氰渣处理和砷固定方向的相关研究和发展趋势。     

Comparison of acid and amyloglucosidase hydrolysis for estimation of non‐structural polysaccharides in feed samples

Enzymatic methods (amyloglucosidase) and methods based on acid solutions (0.1, 0.2 and 0.3 M H₂SO₄ for 1, 2 and 3 h at 100 °C) for the hydrolysis of non‐structural carbohydrates from different feed samples were compared. The monomeric units resulting from the enzymatic and acid hydrolysis were determined by the glucose oxidase and reducing sugar methods. There was a significant effect of acid concentration and of time of hydrolysis on the glucose and reducing sugar values in the hydrolysate. Glucose values were similar for both the amyloglucosidase method and the most intense conditions of hydrolysis (0.3 M for 3 h) for some samples. Under these conditions, however, the reducing sugar values were higher. No acid hydrolysis method was found to estimate correctly the total non‐structural carbohydrates, but α‐linked glucose polymers in biological samples may be determined by sample hydrolysis with a 0.3 M H₂SO₄ solution for 3 h at 100 °C since the glucose in the hydrolysate is determined by the glucose oxidase method and the sucrose content of the sample is negligible. © 1999 Society of Chemical Industry     

Characterisation of cellulose-hydrolysing enzymes from the fungus Bipolaris sorokiniana

Cellulose-hydrolysing enzymes from the phytopathogenic fungus Bipolaris sorokiniana were partially purified and characterised. The enzyme production was variable according to the carbon source. β-Glucosidase and cellobiohydrolase activities were higher by growing the fungus on cellulose than on other carbon sources. Carboxymethyl cellulase production was stimulated by other carbohydrates, mainly lactose. Partial enzyme purification was carried out by liquid chromatography on Sepharose CL4B. The purification was about 17-fold, with a yield of 41% as judged by assay with p-nitrophenyl-β-D -glucopyranoside as substrate. The optimum pH and temperature were 5.0 and 55–60 °C respectively. The enzyme was stable at 28 and 37 °C but lost about 50% of its initial activity after 120 min at 55 °C. Saccharification of cellulosic materials such as crystalline cellulose, filter paper and wheat straws was carried out using the partially purified enzyme, resulting in the production of reducing sugars. © 1999 Society of Chemical Industry     

Pectinolytic and cellulolytic activities of heat resistant fungi and their macerating effects on mango and African mango

Five heat resistant fungi (HRF), Neosartorya fischeri, N fischeri var spinosa, N quadricincta, Paecilomyces varioti and Byssochlamys nivea, were studied for production of pectinolytic and cellulolytic activities. All isolates produced considerable hydrolase, lyase and pectinesterase activities. Hydrolase activities were significantly higher in fruit tissue (mango and African mango) media than in pectin medium (P < 0.01) when assayed by both cup plate and viscometric methods. Activities produced in both fruit media were comparable in N fischeri, N fischeri var spinosa and P varioti but not in N quadricincta and B nivea. All isolates produced greater lyase activities in pectin medium than in fruit tissue media except for N quadricincta, while the converse was the case for pectinesterase. P varioti did not utilise carboxymethyl cellulose or produce cellulase activity. Other isolates produced cellulase with B nivea producing the greatest activity. Each isolate caused considerable maceration of artificially inoculated mango and African mango fruits, which is not directly related to measurable pectinase or cellulase. The possibility of co‐operation between pectinase and cellulase activities in the disintegration of fruit tissues is discussed. © 1999 Society of Chemical Industry     

Enzymes as biocatalysts in the modification of natural lipids

Though designed by nature to effect hydrolysis of lipids, lipases can, under appropriate reaction conditions, promote ester formation through reaction of acids and alcohols (esterification) or of esters with acids (acidolysis), alcohols (alcoholysis), or other esters (interesterification). Compared with chemical processes already carried out on an industrial scale enzymic reactions occur under milder (and ‘greener’) conditions though they may take longer. Of greater significance is the specificity shown by the enzymes which permits the formation of lipid derivatives not easily prepared by conventional laboratory procedures. This review describes the lipases and their various specificities and reports on their use in hydrolysis and in the production of phospholipids, fatty acids, alkyl esters, mono- and di-acylglycerols, triacylglycerols, other esters, and amides. Some of these have already led to marketable products but for the most part the full potential of these reactions has yet to be realised. The reactions of other enzymes promoting interesting reactions at unsaturated centres are also described. © 1999 Society of Chemical Industry