THE DESIGN AND ANALYSIS OF EXPERIMENTS. By Oscar Kempthorne. New York, John Wiley and Sons, Inc., 1952. 631 pp. $8.50. This book by a teacher of statistics (as well as a consultant for \"experimenters\") is a comprehensive study of the philosophical background for the statistical design of experiment. It is necessary to have some facility with algebraic notation and manipulation to be able to use the volume intelligently. The problems are presented from the theoretical point of view, without such practical examples as would be helpful for those not acquainted with mathematics. The mathematical justification for the techniques is given. As a somewhat advanced treatment of the design and analysis of experiments, this volume will be interesting and helpful for many who approach statistics theoretically as well as practically. With emphasis on the \"why,\" and with description given broadly, the author relates the subject matter to the general theory of statistics and to the general problem of experimental inference. MARGARET J. ROBERTSON

The Design and Analysis of Experiments

介绍了Kirk—Othmer Encyclopedia of Chemical Technology（化工技术百科全书）（第五版）电子图书网络版数据库，并对该数据库使用方法和检索途径作出了说明，且结合实例简单地介绍了该数据库的检索方法。

Kirk-Othmer Encyclopedia of Chemical Technology数据库介绍及实例

https://pubs.rsc.org/en/content/articlepdf/2019/CY/C9CY00415G

Novozym 435: the “perfect” lipase immobilized biocatalyst?

Standard methods for the analysis of oils, fats and derivatives. 7th Revised and enlarged edition. Oxford, London, Edinburgh, Boston, Palo Alto, Melbourne: Blackwell Scientific Publication, 1987. 347 pp. 55 Ł, ISBN 0-632-01586-1

Lipase (E.C.3.1.1.3) belongs to the hydrolases and is also known as fat splitting, glycerol ester hydrolase or triacylglycerol acylhydrolase. Lipase catalyzes the hydrolysis of triglycerides converting them to glycerol and fatty acids in an oil-water interface. These are widely used in food, dairy, flavor, pharmaceuticals, biofuels, leather, cosmetics, detergent, and chemical industries. Lipases are of plant, animal, and microbial origin, but microbial lipases are produced at industrial level and represent the most widely used class of enzymes in biotechnological applications and organic chemistry. Phylogenetic analysis and comparison of residues around GxSxG motif provided an insight to the diversity among bacterial lipases. A variety of para-Nitrophenyl (p-NP) esters having C2 to C16 (p-NP acetate to p-NP palmitate) in their fatty acid side chain can be hydrolyzed by bacterial lipases. Large heterogeneity has been observed in molecular and catalytic characteristics of lipases including molecular mass; 19–96 kDa, Km; 0.0064–16.58 mM, Kcat; 0.1665–1.0 × 104 s−1 and Kcat/Km; 26.02–7377 s-1/mM. Optimal conditions of their working temperature and pH have been stated 15–70 °C and 5.0–10.8, respectively and are strongly associated with the type and growth conditions of bacteria. Surface hydrophobicity, enzyme activity, stability in organic solvents and at high temperature, proteolytic resistance and substrate tolerance are the properties of bacterial lipases that have been improved by engineering. Bacterial lipases have been extensively studied during last decade. However, their wider applications demand a detailed review on purification, catalytic characterization and applications of lipases.

Bacterial lipases: A review on purification and characterization.

Lipase can catalyze varieties of reactions at the interface of aqueous and organic phase. Among various alternatives to modify catalytic performance of lipase, the addition of surfactants, particularly nonionic surfactants, has been widely studied. Low concentrations of nonionic surfactants augment lipase catalysis; on increasing surfactant concentration, often the catalytic performance decreases. Mole ratio of water to (nonionic) surfactant also has a profound effect on lipase activity. Catalytic abilities of some lipases are either enhanced or reduced in the presence of all nonionic surfactants of the same type, whereas for some other lipases, nonionic surfactants of the same type have mixed effect. Nonionic surfactant even changes substrate specificity of lipase. Water-in-ionic liquid microemulsion involving nonionic surfactant often performs better than other systems in improving catalytic ability of lipase. Tween and Triton surfactants often enhance enantiomeric separation catalyzed by lipase. Nonionic surfactants significantly affect activities of immobilized lipase, being present either as a component during immobilization or as a component in reaction medium. Lipases coated with nonionic surfactants act better than reverse micelles and microemulsions containing lipase. Thus, nonionic surfactants help lipase catalyzed processes in various media to enhance production of useful compounds like flavor ester, structured lipids, optically pure compounds, and noncrystalline polymers.

Lipase Catalysis in Presence of Nonionic Surfactants

Optimal hydrolysis of mustard oil to erucic acid: A biocatalytic approach

Mixed micelles and bicontinuous microemulsions: Promising media for enzymatic reactions.

Application of mixed surfactants coupled with statistical optimization in lipase catalyzed oil hydrolysis is presented for the first time in this study. Selective hydrolysis of brown mustard oil to erucic acid by porcine pancreas lipase was enhanced by mixed surfactants comprising of an oil-soluble nonionic surfactant (Span 80) and a watersoluble nonionic surfactant (Tween 80). The production of erucic acid was maximized using statistically designed experiments and subsequent analysis of their result by response surface methodology. The most significant variables were enzyme concentration and concentration of Tween 80. Small changes in pH and concentration of Span 80 also produced a significant change in the production of erucic acid. Temperature and speed of agitation were insignificant variables and were fixed at 35oC and 900 rpm, respectively. Under these conditions, the optimal combination of other variables were pH 9.65, 2.13 mg/g enzyme in oil, 9.8 × 10−3 M Span 80 (in oil), and 4 × 10−3 M Tween 80 (in buffer). These conditions led to formation of 99.69% of the total erucic acid in 1.25 h. Interaction of enzyme concentration with pH significantly affected erucic acid production.

Erucic acid production using porcine pancreas lipase: Enhancement by mixed surfactants

This work studied hydrolysis of castor oil to ricinoleic acid, catalyzed by immobilized porcine pancreas lipase (PPL) and impact of surfactant on its augmentation. In immobilization of lipase throu...

Debajyoti Goswami

Papers

Lipase Catalysis in Presence of Nonionic Surfactants

Optimal hydrolysis of mustard oil to erucic acid: A biocatalytic approach

Mixed micelles and bicontinuous microemulsions: Promising media for enzymatic reactions.

Erucic acid production using porcine pancreas lipase: Enhancement by mixed surfactants

Surfactant assisted production of ricinoleic acid using cross-linked and entrapped porcine pancreas lipase