Collagen as a Carrier for Enzymes: Materials Science and Process Engineering Aspects of Enzyme Engineering

Bernath, F. R.; Vieth, W. R.

doi:10.1007/978-1-4684-2088-3_10

Cited by 9 publications

(3 citation statements)

References 9 publications

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“…This effect may be caused by the microenvironmental pH of the chitosan matrix. At high H+ concentrations the amino groups of the chitosan would be protonated, thereby attracting hydroxyl ions which would maintain a higher microenvironmental pH than in the bulk solution and thus stabilize the ,6-glucosidase (2,11). The similarity on the alkaline side of the optimum cannot be so easily explained.…”

Section: Resultsmentioning

confidence: 99%

Immobilization of Aspergillus beta-glucosidase on chitosan

Bissett¹,

Sternberg²

1978

Appl Environ Microbiol

132

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Glucosidase of Aspergillus phoenicis QM 329 was immobilized on chitosan, using the bifunctional agent glutaraldehyde. The most active preparation based on the amount of support contained a 1:2.5 enzyme-to-chitosan ratio (wt/wt). However, the specific activity of the bound enzyme decreased from 10 to 1% with increasing enzyme-to-chitosan ratio. Compared with free f-glucosidase, the immobilized enzyme exhibited: (i) a similar pH optimum but more activity at lower pH values; (ii) improved thermal stability; (iii) a similar response to inhibition by glucose; and (iv) mass transfer limitations as reflected by higher apparent Km and lower energy of activation.

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Section: Resultsmentioning

confidence: 99%

Immobilization of Aspergillus beta-glucosidase on chitosan

Bissett¹,

Sternberg²

1978

Appl Environ Microbiol

132

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“…Only recently have American investigators again begun to publish work on glucose isomerase (e.g., Strandbert andSmiley, 1971, 1972;Vieth, et a1., 1973;Wang and Vieth, 1973;Havewala and Pitcher, 1974;-Pub1ications by workers at Corn Processing Corporation, and Clinton Corn Products cited above). Continuing interest in the study of glucose isomerase in this country is further exemplified by several papers within this volume discussing its immobilization (Olson and Stanley, 1974); Bernath and Vieth, 1974;Kolarik, et a1., 1974). A chronology of many important isomerase patents appears in Table VI and illustrates the increasing interest in this enzyme; this applied work will be reviewed in the following sections.…”

Section: Summary Survey Of Glucose Isomerase Processesmentioning

confidence: 96%

Glucose Isomerase: A Case Study of Enzyme-Catalyzed Process Technology

Hamilton

Colton

Cooney

1974

Immobilized Enzymes in Food and Microbial Processes

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Process engineering considerations important in the exploitation of enzyme-catalyzed reactions for large-scale production of desired products are illustrated in the context of a case study of glucose isomerase technology. The state of the art of glucose isomerase processing as revealed by journal and patent literature is reviewed and assessed. Among topics covered are enzyme production, immobilization and stabilization, kinetics, reactor design, and product recovery. Some possible future processing objectives, such as production of pure fructose, are discussed.

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“…I03143 A highly negative-charged membrane would attract hydrogen ions, maintain a lower microenvironment pH than the bulk solution, and thus stabilize the enzyme in a highly alkaline substrate stream. 119 Immobilized beta-galactosidase to polymethylene polyphenylisocyanate shifted the pH optimum to the alkaline side, indicating that the matrix is negatively charged. 138 The charge of pH-activity profile of tryptopanase by immoblization was caused by the localized proton which was eliminated from the alpha-hydrogen of the amino acid substrate prior to the subsequent rate-determining beta-elimination step.…”

Section: A Immobilized Enzymesmentioning

confidence: 99%

Modification of plant proteins by immobilized proteases

Lee

Lopez

1984

C R C Critical Reviews in Food Science and Nutrition

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A potential application of plant proteins could be a replacement of animal proteins now in use in the food industry on the basis of certain specific functional properties plant proteins have. Modification of the chemical structure of selected plant proteins is needed to replace more expensive animal proteins as food ingredients that have specific functional characteristics. Structure modification may be achieved by physical, chemical, or microbiological methods, or by a combination of these. Immobilized enzyme techniques offer significant advantages for protein modification. Knowledge of the molecular properties of plant proteins is essential to understand the basis of protein functionality, to modify proteins so that they acquire desirable functional properties, and to predict potential applications of modified plant proteins. This paper reviews all the above mentioned aspects of plant protein chemistry and potential utilization.

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Collagen as a Carrier for Enzymes: Materials Science and Process Engineering Aspects of Enzyme Engineering

Cited by 9 publications

References 9 publications

Immobilization of Aspergillus beta-glucosidase on chitosan

Immobilization of Aspergillus beta-glucosidase on chitosan

Glucose Isomerase: A Case Study of Enzyme-Catalyzed Process Technology

Modification of plant proteins by immobilized proteases

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