Publications by authors named "Per Munk Nielsen"

Degumming is an oil refinement process in which the naturally occurring phospholipids in crude vegetable oils are removed. Enzymatic degumming results in higher oil yield and more cost-efficient processing compared to traditional degumming processes using only water or acid. Phospholipase C hydrolyses phospholipids into diglycerides and phosphate groups during degumming.

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Enzymatic degumming is a well established process in vegetable oil refinement, resulting in higher oil yield and a more stable downstream processing compared to traditional degumming methods using acid and water. During the reaction, phospholipids in the oil are hydrolyzed to free fatty acids and lyso-phospholipids. The process is typically monitored by off-line laboratory measurements of the free fatty acid content in the oil, and there is a demand for an automated on-line monitoring strategy to increase both yield and understanding of the process dynamics.

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Enzymatic biodiesel production has been at the forefront of biofuels research in recent decades because of the significant environmental advantages it offers, while having the potential to be as effective as conventional chemically catalyzed biodiesel production. However, the higher capital cost, longer reaction time, and sensitivity of enzyme processes have restricted their widespread industrial adoption so far. It is also posited that the lack of research to bring the biodiesel product into final specification has scuppered industrial confidence in the viability of the enzymatic process.

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In this work, we demonstrate the scale-up from an 80 L fed-batch scale to 40 m(3) along with the design of a 4 m(3) continuous process for enzymatic biodiesel production catalyzed by NS-40116 (a liquid formulation of a modified Thermomyces lanuginosus lipase). Based on the analysis of actual pilot plant data for the transesterification of used cooking oil and brown grease, we propose a method applying first order integral analysis to fed-batch data based on either the bound glycerol or free fatty acid content in the oil. This method greatly simplifies the modeling process and gives an indication of the effect of mixing at the various scales (80 L to 40 m(3) ) along with the prediction of the residence time needed to reach a desired conversion in a CSTR.

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Callera™ Trans L, a liquid formulation of Thermomyces lanuginosus lipase, has recently shown great promise as a cost-efficient catalyst for methanolysis of triglyceride substrates, specifically in the BioFAME process. However, identifying the right combination of temperature and concentrations of catalyst, water and methanol to realize the full potential of the reaction system has remained a challenge. This study presents an investigation of the impact of temperature, enzyme and water concentration on the reaction, as well as the effect of methanol feed rate for the conversion of rapeseed oil in a fed-batch reaction system.

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Background: Enzymatic biodiesel is becoming an increasingly popular topic in bioenergy literature because of its potential to overcome the problems posed by chemical processes. However, the high cost of the enzymatic process still remains the main drawback for its industrial application, mostly because of the high price of refined oils. Unfortunately, low cost substrates, such as crude soybean oil, often release a product that hardly accomplishes the final required biodiesel specifications and need an additional pretreatment for gums removal.

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An integrated biodiesel process that combines enzymatic esterification and alkaline transesterification is suggested. With focus on the enzymatic step, the paper provides proof of concept and suggestions for further process development. Hence, palm fatty acid distillate (PFAD) has been enzymatically converted to fatty acid methyl esters in a two-step process using the immobilized lipase Novozym 435 in packed-bed columns.

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Oxidation of lactose to lactobionic acid by a Microdochium nivale carbohydrate oxidase was studied. The K(m)-value for lactose, obtained by a traditional enzymatic assay, was 0.066 mM at pH 6.

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Enzymatic oxidation of lactose to lactobionic acid (LBA) by a carbohydrate oxidase from Microdochium nivale was studied in a pilot-scale batch reactor of 600 L working volume using a rotary jet head (RJH) for mixing and mass transfer (Nordkvist et al., 2003, Chem Eng Sci 58:3877-3890). Both lactose and whey permeate were used as substrate, air was used as oxygen source, and catalase was added to eliminate the byproduct hydrogen peroxide.

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