Enzymes in food processing

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Otherwise a model is built based on known enzyme structures with homologous sequences [ 90 ]. Computational methods are also welcome in directed evolution, as a tool to better lead the random mutagenesis [ 97 ]. Ultimately this approach is put into practice by producing a site-directed mutant, where selected amino acids are replaced with those suggested from the outcome of modeling.

Some relevant examples of this strategy in the area of food and feed processing are given. Immobilization There are several issues that can be lined up to sustain enzyme immobilization. Table 4 A generalized characterization of immobilization methods. Typical Bioreactors The most common form of enzymatic reactors for continuous operation is the packed-bed setup, basically a cylindrical column holding a fixed bed of catalyst particles Figure 1. Figure 1. References 1. Vasic-Racki D.

Enzymes and their applications in food processing

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Carrez D, Soetaert W. Looking ahead in Europe: white biotech by Industrial Biotechnology. Research and markets Illanes A. Enzyme Biocatalysis—Principles and Applications. Biocatalysis: Fundamentals and Applications. Environment as a new perspective on the use of enzymes in the food industry. Food Science and Technology. Rozzell JD. Commercial scale biocatalysis: myths and realities.

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AMFEP Joint Food Enzymes Dossiers

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Applied Biochemistry and Biotechnology. Bertoldo C, Antranikian G. Starch-hydrolyzing enzymes from thermophilic archaea and bacteria. Current Opinion in Chemical Biology. Sources, properties and suitability of new thermostable enzymes in food processing. Critical Reviews in Food Science and Nutrition. Properties of extremophilic enzymes and their importance in food science and technology. Vieille C, Zeikus GJ. Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability.

Microbiology and Molecular Biology Reviews. Characterization of amylolytic enzyme activities associated with the hyperthermophilic archaebacterium Pyrococcus furiosus. Applied and Environmental Microbiology. I-3 and its use in the direct hydrolysis of raw potato starch.

Enzymes in food processing

Arikan B. Highly thermostable, thermophilic, alkaline, SDS and chelator resistant amylase from a thermophilic Bacillus sp.

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  • GRE1: characterization and gene isolation. World Journal of Microbiology and Biotechnology. Applied Microbiology and Biotechnology. Indian Journal of Biotechnology. Hernalsteens S, Maugeri F. Properties of thermostable extracellular FOS-producing fructofuranosidase from cryptococcus sp. European Food Research and Technology. Properties of a novel thermostable glucoamylase from the hyperthermophilic archaeon sulfolobus solfataricus in relation to starch processing.

    Srih-Belghith K, Bejar S. A thermostable glucose isomerase having a relatively low optimum pH: study of activity and molecular cloning of the corresponding gene. Biotechnology Letters. Glucose-to-fructose conversion at high temperatures with xylose glucose isomerases from Streptomyces murinus and two hyperthermophilic Thermotoga species.

    Journal of Bacteriology. European Journal of Biochemistry. Comparative analysis of thermostability of extracellular inulinase activity from Aspergillus fumigatus with commercially available Novozyme inulinase. Purification and characterization of heat-stable exo-inulinase from Streptomyces sp. Journal of Food Engineering. Thermostable inulinases secreted by yeast and yeast-like strains from the Brazilian semi-arid region.

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    International Journal of Food Sciences and Nutrition. Characterization of a thermostable levansucrase from Bacillus sp. TH capable of producing high molecular weight levan at high temperature.

    Journal of Biotechnology. Kunamneni A, Singh S. Improved high thermal stability of pullulanase from a newly isolated thermophilic Bacillus sp.

    Application of Enzymes in food industry

    Winterhalter C, Liebl W. Two extremely thermostable xylanases of the hyperthermophilic bacterium Thermotoga maritima MSB8. Khandeparkar R, Bhosle NB.

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