Abstract
An affinity ultrafiltration process has been developed by exploiting affinity binding in conjunction with cross‐flow filtration. The process was proven to possess high resolution, high recovery yield, and ease of scale‐up. The process could purify trypsin from a trypsin‐chymotrypsin mixture batchwise or continuously. Essential for applying this concept was the synthesis of a water‐soluble high‐molecular‐weight polymer bearing m‐aminobenzamidine, a strong and specific trypsin in hibitor. A mathematical model was also developed to describe the dynamic behavior of the newly developed purification process. The model was able to predict the profiles of enzyme concentrations in the process with high accuracy.
| Original language | English |
|---|---|
| Pages (from-to) | 451-459 |
| Number of pages | 9 |
| Journal | Biotechnology and Bioengineering |
| Volume | 32 |
| Issue number | 4 |
| DOIs | |
| Publication status | Published - 5 Aug 1988 |
| Externally published | Yes |