碱性果胶酶的生物制造及其在纺织工业清洁生产中的应用研究进展

以下综述了碱性果胶酶的生物制造及其在纺织工业清洁生产中的应用研究进展。微生物发酵法是目前生产碱性果胶酶的主要方式,枯草芽孢杆菌是碱性果胶酶工业发酵生产中效果较好的野生菌株。影响发酵法生产碱性果胶酶的主要因素有:底物浓度及其流加方式、细胞浓度、搅拌转速、通气速率、pH、温度等。构建基因工程菌为碱性果胶酶的发酵生产开辟了一条有效途径,其中重组毕赤酵母的产酶水平最高,在10吨发酵罐上酶活达1305U/mL。碱性果胶酶可用于棉织物前处理的精练工艺,与传统高温碱煮相比,具有保护纤维、提高精练效率、降低能耗和污染的优势。通过分子定向进化技术对碱性果胶酶进行分子改造,使其催化特性更加适合于纺织精练工艺,进而实现纺织工业的清洁生产是未来的研究重点和热点。     

微生物果胶酶研究进展

果胶酶是一类分解果胶质的酶的总称,它能将复杂的果胶分解为半乳糖醛酸等小分子。目前果胶酶在食品、纺织、医药、造纸、环境、生物技术、饲料等领域得到广泛应用。果胶酶主要来自微生物。综述了微生物果胶酶生产菌的菌种、选育、鉴定、发酵方法和发酵条件优化,酶的分离纯化、酶学性质和分子生物学方面的研究进展,并介绍了果胶酶的应用进展,最后展望了微生物果胶酶研究的广阔前景。     

微生物果胶酶研究及其在果蔬加工中的应用进展

果胶酶是指分解果胶物质的多种酶的总称。果胶酶分布很广,可来源于动物、植物和微生物。果胶酶在工业生产领域中是一种重要的新兴酶类,在果蔬加工、饲料、纺织和造纸工业中应用非常广泛。本文介绍了果胶酶的微生物来源、分类及其在果蔬加工中的应用进展。     

细菌果胶酶的研究进展

近些年来,国内外对细菌果胶酶的研究取得了很大的进展,产果胶酶的新细菌菌种不断地被发现,细菌果胶酶新的应用领域不断地被拓宽。细菌所产的果胶酶多为碱性,具有较好的热稳定性和较宽的酸碱作用范围,被广泛应用于麻类的生物脱胶、茶与咖啡发酵、造纸和果胶废水处理等领域中。细菌果胶酶工业生产具有投资少、成本低、无环境污染等优点。简要概述产生果胶酶的细菌种类、细菌果胶酶的分类、已克隆的酶基因以及应用等内容。     

酵母发酵生产辅酶Q10提取方法研究进展

辅酶Q10是存在于哺乳动物中,能与酶蛋白形成复合物以发挥酶学活性的有机小分子化合物,目前广泛应用于医药、日化、保健、食品等不同领域。辅酶Q10来源丰富,其中酵母是其工业生产的主要来源之一。广受关注的酵母发酵生产辅酶Q10的提取分离手段不断革新,产量不断增加,处理方式更加环保,应用日渐拓宽。本文就近年来国内外酵母发酵生产辅酶Q10的提取分离方法进行了综述,包括酵母菌种的类型与优化、辅酶Q10提取检测方法、工业生产放大工艺以及与产品质量相关的各个影响因素,并对酵母发酵生产辅酶Q10的前景进行了展望。     

产酸性果胶酶的研究应用及展望

果胶酶是分解果胶的酶,是复合酶。果胶酶分布广泛,植物、微生物、原生动物以及昆虫中都有存在。细菌、放线菌、酵母和霉菌都是工业生产领域中合成果胶酶的主要产生菌,本文综述了产酸性果胶酶的研究现状。     

黑曲霉HG-1发酵苹果渣生产果胶酶的工艺优化及部分酶学性质

目的：采用价格低廉的农业废弃物苹果渣为主要原料生产果胶酶,优化其生产工艺,并对果胶酶的部分酶学性质进行研究。方法：以黑曲霉HG-1为生产菌种,采用单因子实验和正交试验进行固态发酵。结果：最适培养基为苹果渣10g、棉粕10g、（NH4）2SO40.2g、K2HPO40.06g、初始水分含量60%;最适发酵条件为装料量为20g干料/250ml三角瓶,30℃恒温培养48h,果胶酶酶活力可达22248U/g。果胶酶酶促反应最适温度为45℃,最适pH为5.0;在50℃以下,pH3.0～6.0时稳定性良好;Ca^2＋、Mg^2＋、Fe^2＋对该酶有激活作用,而Ba^2＋、Mn^2＋、Zn^2＋有抑制作用。结论：以苹果渣代替麸皮作为黑曲霉HG-1固态发酵生产果胶酶的主要原料在技术上具有可行性,可大幅度降低生产成本;同时还可以部分解决苹果渣的综合利用问题。     

酶的固体发酵生产研究进展

由于固体发酵具有基质来源广泛、能耗少、对环境友好和生产成本低等特点,在酶的生产中仍得到较广泛的应用.介绍了固体发酵产酶的种类和产酶微生物,基质来源及发酵条件控制技术等方面的进展,总结了固体发酵产酶存在的问题,并提出了今后该领域的研究方向.     

α-L-鼠李糖苷酶特性简述及影响酶活的因素

α-L-鼠李糖苷酶是一个非常重要的工业酶,广泛分布于各种生物中。不同来源的α-L-鼠李糖苷酶具有多样性。细菌来源的α-L-鼠李糖苷酶的最适pH接近中性或偏碱性,而真菌来源的α-L-鼠李糖苷酶的最适pH在酸性范围。除此之外,不同来源的α-L-鼠李糖苷酶在最适温度、热稳定性和底物特异性等方面也不尽相同,酶学性质的差异,决定了其在工业应用时所具有的优势和限制。因此,分析不同来源的α-L-鼠李糖苷酶的酶学性质、阐明其在催化机制和底物特异性等方面的异同点、探究底物的糖苷配体和金属阳离子对酶活性的影响以及L-鼠李糖和葡萄糖对酶的竞争性抑制作用,可以为工业生产中准确选择α-L-鼠李糖苷酶提供参考,进一步推动该酶的工业化应用进程。     

细菌漆酶的研究及应用进展北大核心CSCD

漆酶作为一种绿色环保的多酚氧化酶类,目前被广泛地应用于染料降解、造纸等领域。细菌漆酶与真菌漆酶相比,有更好的热稳定性和更宽的最适pH范围。因此,在工业应用方面更具优势与潜力。综述细菌漆酶的来源、分布、分子结构等基本信息,以及目前细菌漆酶发酵生产水平,并对固定化细菌漆酶进行总结。此外,对细菌漆酶在染料废水、电化学应用及造纸等工业生产方面的应用作简要的介绍。     

产果胶酶菌株的筛选

从不同来源的生物样品中分离到产果胶酶菌株,采用刚果红染色法和十六烷基三甲基溴化铵沉淀法进行初筛,通过摇瓶发酵试验进行复筛,最终获得2株果胶酶活力较高的细菌G16和G25,其酶活力分别达到6．37万U／mL和6．84万U／mL。     

Recent advancements in the production and application of microbial pectinases: an overview

The wide utility and catalytic efficiency of microbial pectinase in various industries has greatly increased its global demand. Among the natural sources of pectinases, microbial pectinases are used frequently for its ease of production and unique physicochemical properties. Yet similar to other industrial enzymes, pectinases also face the constraint of thermo-tolerance and low yield in its economised production. The current review addresses the various strategies adopted to meet the high yield and thermo-tolerance of pectinases as well as the various attempts made in the field of pectinases to its improved production and better catalytic efficiency. The utilisation of natural as well as recombinant microbial sources, metagenomic approaches, metabolic engineering, site directed mutagenesis and media engineering techniques adopted in the field of pectinases have been discussed. The significance of pectinases in various industries is depicted by enlisting its applications. To the best our knowledge the current review is unique being the first attempt to compile the recent advancements in the field of pectinases.     

果胶酶分离纯化及分析方法的研究进展

果胶酶能降解果胶质,在果汁制造、果酒酿造等方面有着广泛应用。果胶酶分子生物学的迅速发展极大地促进了分离纯化与分析方法的研究。由于不同菌种产生的果胶酶成分复杂程度不同,分离纯化手段和分析方法也不相同。本文对果胶酶分离纯化手段及其分析方法进行了综述。     

Validation of leaf and microbial pectinases: commercial launching of a new platform technology

Almost all current genetically modified plant commercial products are derived from seeds. The first protein product made in leaves for commercial use is reported here. Leaf pectinases are validated here with eight liquid commercial microbial enzyme products for textile or juice industry applications. Leaf pectinases are functional in broad pH/temperature ranges as crude leaf extracts, while most commercial enzyme products showed significant loss at alkaline pH or higher temperature, essential for various textile applications. In contrast to commercial liquid enzymes requiring cold storage/transportation, leaf pectinase powder was stored up to 16 months at ambient temperature without loss of enzyme activity. Commercial pectinase products showed much higher enzyme protein PAGE than crude leaf extracts with comparable enzyme activity without protease inhibitors. Natural cotton fibre does not absorb water due to hydrophobic nature of waxes and pectins. After bioscouring with pectinase, measurement of contact‐angle water droplet absorption by the FAMAS videos showed 33 or 63 (leaf pectinase), 61 or 64 (commercial pectinase) milliseconds , well below the 10‐second industry requirements. First marker‐free lettuce plants expressing pectinases were also created by removal of the antibiotic resistance aadA gene. Leaf pectinase powder efficiently clarified orange juice pulp similar to several microbial enzyme products. Commercial pilot scale biomass production of tobacco leaves expressing different pectinases showed that hydroponic growth at Fraunhofer yielded 10 times lower leaf biomass per plant than soil‐grown plants in the greenhouse. Pectinase enzyme yield from the greenhouse plants was double that of Fraunhofer. Thus, this leaf‐production platform offers a novel, low‐cost approach for enzyme production by elimination of fermentation, purification, concentration, formulation and cold chain.     

Hydrolysis of grapefruit peel waste with cellulase and pectinase enzymes

Approximately 1 million metric tons of grapefruit were processed in the 2003/04 season resulting in 500,000 metric tons of peel waste. Grapefruit peel waste is usually dried, pelletized, and sold as a low-value cattle feed. This study tested different loadings of commercial cellulase and pectinase enzymes and pH levels to hydrolyze grapefruit peel waste to produce sugars. Pectinase and cellulase loadings of 0, 1, 2, 5, and 10mgprotein/g peel dry matter were tested at 45 degrees C. Hydrolyses were supplemented with 2.1mg beta-glucosidase protein/g peel dry matter. Five mg pectinase/g peel dry matter and 2mgcellulase/g peel dry matter were the lowest loadings to yield the most glucose. Optimum pH was 4.8. Cellulose, pectin, and hemicellulose in grapefruit peel waste can be hydrolyzed by pectinase and cellulase enzymes to monomer sugars, which can then be used by microorganisms to produce ethanol and other fermentation products.     

Production of pectinolytic enzymes pectinase and pectin lyase by <Emphasis Type="Italic">Bacillus subtilis</Emphasis> SAV-21 in solid state fermentation

Pectin-degrading enzymes (pectinase and pectin lyase) were produced in solid state fermentation by Bacillus subtilis SAV-21 isolated from fruit and vegetable market waste soil of Yamuna Nagar, Haryana, India, and identified by 16S rDNA sequencing. Under optimized conditions, maximum production of pectinase (3315 U/gds) and pectin lyase (10.5 U/gds) was recorded in the presence of a combination of orange peel and coconut fiber (4:1), with a moisture content of 60% at 35 °C and pH 4.0 after 4 days and 8 days of incubation, respectively. Pectinase yield was enhanced upon supplementation with galactose and yeast extract, whereas pectin lyase production was unaffected by adding carbon and nitrogen source to the basal medium. Thus, B. subtilis SAV-21 can be exploited for cost-effective production of pectinase and pectin lyase using agro-residues.     

Lactic acid bacteria as a tool for biovanillin production: A review

Vanilla is the most commonly used natural flavoring agent in industries like food, flavoring, medicine, and fragrance. Vanillin can be obtained naturally, chemically, or through a biotechnological process. However, the yield from vanilla pods is low and does not meet market demand, and the use of vanillin produced by chemical synthesis is restricted in the food and pharmaceutical industries. As a result, the biotechnological process is the most efficient and cost-effective method for producing vanillin with consumer-demanding properties while also supporting industrial applications. Toxin-free biovanillin production, based on renewable sources such as industrial wastes or by-products, is a promising approach. In addition, only natural-labeled vanillin is approved for use in the food industry. Accordingly, this review focuses on biovanillin production from lactic acid bacteria (LAB), which is generally recognized as safe (GRAS), and the cost-cutting efforts that are utilized to improve the efficiency of biotransformation of inexpensive and readily available sources. LABs can utilize agro-wastes rich in ferulic acid to produce ferulic acid, which is then employed in vanillin production via fermentation, and various efforts have been applied to enhance the vanillin titer. However, different designs, such as response surface methods, using immobilized cells or pure enzymes for the spontaneous release of vanillin, are strongly advised.