Lactase and other enzymes bound to chitin with glutaraldehyde
| Autor: | William L. Stanley, G. G. Watters, J. M. Mercer, Bock G. Chan |
|---|---|
| Rok vydání: | 1975 |
| Předmět: |
chemistry.chemical_classification
Chromatography biology medicine.medical_treatment Acid phosphatase Bioengineering Lactase Titratable acid Pronase Applied Microbiology and Biotechnology Lactase activity chemistry.chemical_compound Enzyme chemistry Biochemistry Chitin medicine biology.protein Glutaraldehyde Biotechnology |
| Zdroj: | Biotechnology and Bioengineering. 17:315-326 |
| ISSN: | 1097-0290 0006-3592 |
| DOI: | 10.1002/bit.260170303 |
| Popis: | Acid tolerant lactase (I), α-chymotrypsin (II), and acid phosphatase (III) were immobilized on chitin with glutaraldehyde. Pretreatments of the chit in with acid, alkali, ammonia, and pronase were compared with respect to release of titratable amino groups and ability to retain lactase activity. Shrimp chitin appeared to be more sensitive to pretreatment conditions and so effort was concentrated on crab. An acid-alkali pretreatment was selected as most practical and economical, and the properties of enzymes fixed on crab chitin were studied intensively. The pH optima of the fixed enzymes were shifted about one pH unit; the shift for I was toward more acid pH, for II was toward alkaline pH, and for III was toward acid pH. The retained activity of immobilized I was approximately 60% that of the native enzyme. A column in continuous operation with I on chitin-glutaraldehyde gave an apparent activity half-life of 27 days. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text