新型酶制剂———碱性脂肪酶可实现国产化

在洗涤剂中加入酶可以提高去污能力、降低表面活性剂和三聚磷酸钠的用量;使洗涤剂朝低磷或无磷化的方向发展、减少环境污染、发挥洗涤的新功能;酶做为一种生物制品,无毒并能完全生物降解、对环境的生态平衡起良性的作用。因此酶在合成洗涤剂产品中的应用是合成洗涤剂工业发展过程中重大技术进步之一。目前在发达国家里,如日本、美国,所谓“加酶洗涤剂”的商品概念已经淡化,这是由于酶在洗涤剂产品中的地位已经从一种功能性添加物发展为必备的组分,１９９９年全世界工业酶制剂市场达到１６亿美元,其中洗涤剂用酶占３４％,达到５．４…     

乡村城镇化水污染的生态风险及背景警戒值的研究

对江南地区乡村城镇化引起水污染的生态风险进行定量估测与相关分析表明 ,地表水BOD5、NO 3 N、苯酚、表面活性剂和降水 pH、Pb、NO 2 N、苯酚及地下水NO 3 N等水质参数与小城镇人口总数存在着一元线性显著正相关 ,地下水氯化物、细菌总数、洗涤剂和地表水CODCr等水质参数与小城镇人口总数存在着指数显著正相关 ,地表水BOD5、苯酚、表面活性剂和地下水NO 3 N、氯化物、细菌总数、洗涤剂及降水pH、苯酚、Pb等水质参数与小城镇人口密度存在着一元线性显著正相关 ,降水NO 2 N与小城镇人口密度存在着指数显著正相关 .并对该地区小城镇人口的背景极限值和最大允许背景密度进行了推算 .     

表面活性素的发酵生产及应用

表面活性剂（ｓｕｒｆａｃｔａｎｔ）素有“工业味精”之称,它在各个工业领域中具有特殊重要地位。迄今为止,表面活性素（ｓｕｌｆａＣｈｎ）是已发现的最强的一类生物表面活性剂（ｂｉＯＳＬｌｒｉｂｅｂｏｔ）,随着环保意识日益加强,可生物降解的表面活性剂愈来愈受到广泛关注,作为来源于生物体又可为生物所降解,且活性很强的表面活性素可用在洗涤剂制造、油类回收、感光乳剂稳定、植物病害控制、细胞破碎及微生物数量的快速测定等方面。人们在对其结构特性及其生物合成机制进行研究的同时,亦从发酵的角度,对表面活性素的生产及应…     

生物表面活性剂——表面活性素

生物表面活性剂是由微生物在一定条件下合成的具有表面活性的物质,具有对环境无毒、生物降解性能好等特性,广泛应用于洗涤剂、化妆品、食品、医药、石油等工业领域及农业和环境保护方面。该文对表面活性素的生产、结构、性质及应用方面进行了综述。     

碱性蛋白酶

碱性蛋白酶在洗涤剂、制革、丝绸、饲料、医药、食品、环保等领域被广泛应用,具有重要的工业和经济价值。在筛选新型蛋白酶产酶菌株方面,近年来已报道了具有较高pH适应性的碱性蛋白酶,碱性弹性蛋白酶,水解多种底物的碱性蛋白酶,具有耐热、耐表面活性剂、耐氧化剂等特     

酶法合成表面活性剂

用生物技术来研制表面活性剂是当前国际生物工程领域中发展起来的一个新课题。本文概述了用酶法合成五种类型的表面活性剂,单酰化甘油酯类表面活性剂,糖酯类表面活性剂,氨基酸类表面活性剂,磷酯类表面活性剂及氨基酸糖类表面活性剂。     

脂肪醇制备研究进展

脂肪醇是合成表面活性剂、洗涤剂、增塑剂及其他多种精细化学用品的基础化工原料,广泛应用于纺织、日化、造纸、食品、医药、皮革等领域。本文介绍了脂肪醇的市场现状,综述了工业制备脂肪醇的传统方法,阐述了以可再生非粮生物质为原料,利用生物法制备生物基脂肪醇的方法,并对生物基脂肪醇的新合成路线的发展方向进行展望。     

微生物表面活性剂应用新进展

表面活性剂是一种重要的工业原料,微生物表面活性剂是表面活性剂的一种,由于其来源于微生物,具有高效且低毒的特点,是一种环境友好型的表面活性剂,逐渐成为近年来表面活性剂研究的热点,并已在多个领域进行了应用尝试。该文从不同类型的微生物表面活性剂入手,阐述近几年来不同类型的微生物表面活性剂在不同领域的应用,比较了不同种类微生物表面活性剂的应用现状,同时对微生物表面活性剂应用存在的问题进行了分析,并对微生物表面活性剂未来的发展趋势进行了展望。     

微生物表面活性剂应用新进展北大核心

表面活性剂是一种重要的工业原料,微生物表面活性剂是表面活性剂的一种,由于其来源于微生物,具有高效且低毒的特点,是一种环境友好型的表面活性剂,逐渐成为近年来表面活性剂研究的热点,并已在多个领域进行了应用尝试。该文从不同类型的微生物表面活性剂入手,阐述近几年来不同类型的微生物表面活性剂在不同领域的应用,比较了不同种类微生物表面活性剂的应用现状,同时对微生物表面活性剂应用存在的问题进行了分析,并对微生物表面活性剂未来的发展趋势进行了展望。     

生物表面活性剂的合成与提取研究进展*

生物表面活性剂（Biosurfactant）是由微生物产生的具有高表面活性的生物分子。相对于化学合成的表面活性剂,生物表面活性剂对生态系统的毒性较低,且可生物降解。因此,生物表面活性剂开始应用于环境污染治理的各个方面。中从生物表面活性剂生产菌的筛选、培养基的优化及生物表面活性剂的提取等方面对近年来生物表面活性剂的研究进展进行了总结,并对未来的发展方向作了展望。     

A surfactant-coated lipase immobilized in magnetic nanoparticles for multicycle ethyl isovalerate enzymatic production

Gum arabic coated magnetic Fe₃O₄ nanoparticles (GAMNP) were prepared by chemical co-precipitation method and their surface morphology, particle size and presence of polymer-coating was confirmed by various measurements, including transmission electron microscopy (TEM), X-ray diffraction (XRD), thermo gravimetric analysis (TGA), and Fourier transform infra red (FTIR) analysis. Magnetic particles were employed for their potential application as a support material for lipase immobilization. Glutaraldehyde was used as a coupling agent for efficient binding of lipase onto the magnetic carrier. For this purpose, the surface of a Candida rugosa lipase was initially coated with various surfactants, to stabilize enzyme in its open form, and then immobilized on to the support. This immobilized system was used as a biocatalyst for ethyl isovalerate, a flavor ester, production. The influence of various factors such as type of surfactant, optimum temperature and pH requirement, organic solvent used, amount of surfactant in coating lipase and effect of enzyme loadings on the esterification reaction were systematically studied. Different surfactants were used amongst which non-ionic surfactant performed better, showing about 80% esterification yield in 48 h as compared to cationic/anionic surfactants. Enhanced activity due to interfacial activation was observed for immobilized non-ionic surfactant–lipase complex. The immobilized surfactant coated lipase activity was retained after reusing seven times.     

On the mechanism of bacteriorhodopsin solubilization by surfactants

Purple membrane bacteriorhodopsin can be easily solubilized by Triton X-100 and other detergents, but not by deoxycholate. In order to understand this behavior, we have examined the effects of a variety of surfactants. We show that detergents containing the cholane ring (cholate, taurocholate, 3[(3-cholamidopropyl)diethyl-ammonio]propanesulfonic acid...) are virtually unable to solubilize native bacteriorhodopsin. However, when the protein is reconstituted in dimyristoyl phosphatidylcholine and solubilization is assayed at a temperature such that bacteriorhodopsin is in the form of monomers, solubilization by cholane detergents does occur. We propose that steric factors prevent access of the rigid planar surfactant molecules to the hydrophobic protein regions. These are perhaps located in the monomer-monomer interface, whose solvation by surfactants is essential for solubilization to occur. We note that the capacity of some detergents to solubilize bacteriorhodopsin is always associated within the same range of surfactant concentrations with bleaching (partial or total) of the protein chromophore. The detergent-induced bleaching is at least partially reversible, suggesting that free retinal remains associated to some membrane components. While some surfactant molecules remain tightly bound to the membrane protein, cholane detergents can be completely removed from bacteriorhodopsin. Our results indicate that a structure-function relationship exists for detergents applied to the solubilization of bacteriorhodopsin.     

Production of lipase and protease from an indigenous Pseudomonas aeruginosa strain and their evaluation as detergent additives: compatibility study with detergent ingredients and washing performance

An indigenous Pseudomonas aeruginosa strain has been studied for lipase and protease activities for their potential application in detergents. Produced enzymes were investigated in order to assess their compatibility with several surfactants, oxidizing agents and commercial detergents. The crude lipase appeared to retain high activity and stability in the presence of several surfactants and oxidizing agents and it was insusceptible to proteolysis. Lutensol? XP80 and Triton? X-100 strongly activated the lipase for a long period (up to 40 and 30% against the control after 1h) while the protease activity was enhanced by the addition of Triton? WR1339 and Tween? 80. The washing performance of the investigated surfactants was significantly improved with the addition of the crude enzyme preparation. Studies were further undertaken to improve enzymes production. The optimization of fermentation conditions led to an 8-fold increase of lipase production, while the production of protease was enhanced by 60%.     

Interactions of fluorinated surfactants with diphtheria toxin T-domain: testing new media for studies of membrane proteins

The principal difficulty in experimental exploration of the folding and stability of membrane proteins (MPs) is their aggregation outside of the native environment of the lipid bilayer. To circumvent this problem, we recently applied fluorinated nondetergent surfactants that act as chemical chaperones. The ideal chaperone surfactant would 1), maintain the MP in solution; 2), minimally perturb the MP's structure; 3), dissociate from the MP during membrane insertion; and 4), not partition into the lipid bilayer. Here, we compare how surfactants with hemifluorinated (HFTAC) and completely fluorinated (FTAC) hydrophobic chains of different length compare to this ideal. Using fluorescence correlation spectroscopy of dye-labeled FTAC and HFTAC, we demonstrate that neither type of surfactant will bind lipid vesicles. Thus, unlike detergents, fluorinated surfactants do not compromise vesicle integrity even at concentrations far in excess of their critical micelle concentration. We examined the interaction of surfactants with a model MP, DTT, using a variety of spectroscopic techniques. Site-selective labeling of DTT with fluorescent dyes indicates that the surfactants do not interact with DTT uniformly, instead concentrating in the most hydrophobic patches. Circular dichroism measurements suggest that the presence of surfactants does not alter the structure of DTT. However, the cooperativity of the thermal unfolding transition is reduced by the presence of surfactants, especially above the critical micelle concentration (a feature of regular detergents, too). The linear dependence of DTT's enthalpy of unfolding on the surfactant concentration is encouraging for future application of (H)FTACs to determine the stability of the membrane-competent conformations of other MPs. The observed reduction in the efficiency of Förster resonance energy transfer between donor-labeled (H)FTACs and acceptor-labeled DTT upon addition of lipid vesicles indicates that the protein sheds the layer of surfactant during its bilayer insertion. We discuss the advantages of fluorinated surfactants over other types of solubilizing agents, with a specific emphasis on their possible applications in thermodynamic measurements.     

Stripping of nonionic surfactants from the coacervate phase of cloud point system for lipase separation by Winsor II microemulsion extraction with the direct addition of alcohols

Extractive microbial fermentation of lipase by Serratia marcescens ECU1010 in cloud point system was previously carried out in the cloud point system. The direct addition of different alcohols, including iso-butanol, 2-phenylethanol and 1-octanol, into the coacervate phase of the clear supernatant of the fermentation broth formed microemulsion, where the nonionic surfactants and lipase were unevenly partitioned between the different phases in the microemulsion system. The polarity of alcohols strongly affected the microemulsion type at room temperature condition. The results indicated that the Winsor II microemulsion, formed by the addition of iso-butanol or 2-phenylethanol as the organic solvent, favored the stripping of the nonionic surfactant into the O_m phase, whereas the lipase was left in the excess aqueous phase. However, the Winsor I microemulsion, formed by the addition of 1-octanol as the organic solvent, failed to separate the lipase from the nonionic surfactant in the coacervate phase of cloud point system, because the nonionic surfactant and lipase were partitioned into the W_m phase at the same time. Moreover, in the Winsor II microemulsion extraction with 2-phenylethanol as the organic solvent, in which case the protein–surfactant complexes were absent at the interface between the O_m phase and the excess aqueous phase, the high lipase recovery (above 80%) and good nonionic surfactant removal were achieved. The effect of nonionic surfactants on lipase activity was also presented.     

Effectiveness of surfactants in the microbial degradation of oil

Nonionic surfactants increase the rate of selective hydrocarbon utilization by Acinetobacter SL1. Within an homologus series of nonionic surfactants, growth on and utilization of a model oil by Acinetobacter SL1 is dependent upon the surfactant hydrophile‐lipophile balance (HLB). Biological effectiveness of the surfactants apparently is related to the degree of micelle formation by the surfactant in the aqueous phase. A simple algebraic expression describing the response of Acinetobacter SL1 to surfactant concentration gives a measure of the biological effectiveness of an individual surfactant. A cationic and an anionic surfactant inhibited the growth of Acinetobacter SL1 and Pseudomonas SL6 on hydrocarbon substrates. These results are discussed in relation to the selection of suitable detergents for increasing the effective biodegradation of pollutant oil in aquatic habitats.     

Utility of enzymes from <Emphasis Type="Italic">Fibrobacter succinogenes</Emphasis> and <Emphasis Type="Italic">Prevotella ruminicola</Emphasis> as detergent additives

In this study, we investigated the application of cellulase and protease purified from rumen bacteria as detergent additives. Cellulase and protease were purified from the rumen cellulytic bacteria Fibrobacter succinogenes S85, and Prevotella ruminicola 23, respectively. An inhibitor test indicated that the purified protease belongs to the category of serine proteases and metalloproteases. Both the enzymes were effective at a high temperature (50 degrees C) and neutral pH (pH 7-8), but the protease activity increased with the increase in temperature and pH. The purified protease was treated with ten types of surfactants/detergents; it was found to retain over 60% of its activity in the presence of anionic and nonionic detergents. The cellulose plus protease combination was still effective after treatment with Triton X-100 and Tween 80, but the residual activity was low after treatment with Tween 20 than that after treatment with other nonionic detergents. Washing tests indicated that enzyme addition produced no significant improvement in the removal of grass stains, but individual enzyme addition in surfactants/detergents, especially in nonionic detergents, could improve the washing performance of the detergents by improving its ability to remove blood stains. This suggested that the surfactant/detergent class, enzyme properties, and the mixing ratio of ingredients should be considered simultaneously to enhance the washing performance.     

洋葱伯克霍尔德菌脂肪酶：一种应用前景广阔的生物催化剂

洋葱伯克霍尔德菌脂肪酶对有机溶剂（醇）、热、氧化剂、表面活性剂、去污剂、蛋白酶等具有良好的抗性,在有机合成、对映体拆分、非水相催化等领域应用十分广泛。综述了洋葱伯克霍尔德菌脂肪酶的发酵生产、分离纯化、基因克隆与表达、固定化与生物印迹、蛋白质结构解析及应用研究等,并展望了其未来发展方向,以期为该工业酶的研发与广泛应用提供参考。     

Surfactant-modified yeast whole-cell biocatalyst displaying lipase on cell surface for enzymatic production of structured lipids in organic media

The cell surface engineering system, in which functional proteins are genetically displayed on microbial cell surfaces, has recently become a powerful tool for applied biotechnology. Here, we report on the surfactant modification of surface-displayed lipase to improve its performance for enzymatic synthesis reactions. The lipase activities of the surfactant-modified yeast displaying Rhizopus oryzae lipase (ROL) were evaluated in both aqueous and nonaqueous systems. Despite the similar lipase activities of control and surfactant-modified cells in aqueous media, the treatment with nonionic surfactants increased the specific lipase activity of the ROL-displaying yeast in n-hexane. In particular, the Tween 20-modified cells increased the cell surface hydrophobicity significantly among a series of Tween surfactants tested, resulting in 8–30 times higher specific activity in organic solvents with relatively high log P values. The developed cells were successfully used for the enzymatic synthesis of phospholipids and fatty acid methyl esters in n-hexane, whereas the nontreated cells produced a significantly low yield. Our results thus indicate that surfactant modification of the cell surface can enhance the potential of the surface-displayed lipase for bioconversion.     

Ethoxylated alcohol (Neodol-12) and other surfactants in the assay of protein kinase C

Most commonly used surfactants were found to be inhibitors of partially purified rat brain protein kinase C at or above their critical micellar concentrations (CMC). These include sodium lauryl sulfate, deoxycholate, octyl glucoside, dodecyl trimethylammonium bromide, linear alkylbenzene sulfonate and Triton X-100. Several detergents, including the nonionic surfactants digitonin and Neodol-12 (ethoxylated alcohol), did not inhibit protein kinase C activity, even at concentrations greater than their CMC, while the anionic surfactant, AEOS-12 (ethoxylated alcohol sulfate), inhibited enzyme activity only slightly (less than 8%). Since these latter surfactants have little or no inhibitory effect on protein kinase C, they may be of value in solubilizing cells and tissues for the determination of enzyme activity in crude extracts. Among the detergents tested, sodium lauryl sulfate and linear alkylbenzene sulfonate significantly stimulated protein kinase C activity in the absence of phosphatidylserine and calcium. This was found to be dependent on the presence of histone in the protein kinase C assay. These detergents failed to stimulate protein kinase C activity when endogenous proteins in the partially purified rat brain extracts were used as the substrate. Our results indicate that activity of protein kinase C can be modified by the conditions of the assay and by the detergents used to extract the enzyme.