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Title: Investigation of the nature of semisynthetic esterases: Final report for the period September 15, 1981 to December 31, 1986

Technical Report ·
OSTI ID:7094315

Semisynthetic enzymes (SSE) have been prepared by chemical means. The procedure consists of perturbing the tertiary structure of a protein, adding a modifier and crosslinking with a bifunctional reagent. In the study reported herein the protein is ribonuclease (RNase), the modifiers are indole derivatives and the bifunctional reagent is glutaralydehyde. The process results in the generation of semisynthetic esterases particularly effective in catalyzing the hydrolysis of aromatic amino acid esters. The low solubility of many of the indole derivatives used as modifiers limits the yield of SSE. Five hydroxy indole carboxylic acids are particularly effective. In addition these derivatives are more soluble than many of the other commerically available indole derivatives. The crude mixture of SSE was purified by classical methods which resulted in the identification of two types of esterases. One group has a pH optimum at about pH 6 while the optimum for the other group is at 7.5. Purification on DEAE Sephadex indicates the presence of several SSE in each group each possessing its own unique substrate specificity. 20 refs., 15 figs., 14 tabs.

Research Organization:
Anatrace, Inc., Maumee, OH (USA)
DOE Contract Number:
AC02-81ER12003
OSTI ID:
7094315
Report Number(s):
DOE/ER/12003-9; ON: DE87005780
Resource Relation:
Other Information: Portions of this document are illegible in microfiche products
Country of Publication:
United States
Language:
English