1172-66-3Relevant academic research and scientific papers
Pronase catalysed peptide syntheses
Lobell, Mario,Schneider, Manfred P.
, p. 319 - 325 (2007/10/03)
A mixture of proteases from Streptomyces griseus (pronase), displaying a very broad substrate tolerance in the hydrolysis of peptides, has been studied for the first time systematically regarding their substrate specificity in peptide synthesis. It is demonstrated that pronase can be employed successfully for the formation of dipeptides with yields up to 95%. Pronase has also been employed successfully as catalyst for the enzyme assisted synthesis of a hexapeptide.
Immobilized Aspergillus Oryzae Protease Catalyzed Formation of Peptide Bonds in Organic Solvent
Shih, Ing-Lung,Lin, Yun-Yin,Huang, Hui-Yao,Tai, Dar-Fu,Chen, Kuan-Chu
, p. 327 - 330 (2007/10/03)
Immobilized Aspergillus oryzae protease (AOP) catalyzed the formation of peptide bonds between N-protected amino acids and amino acid esters or amides in ethyl acetate. The influences of pH and reaction time on the coupling of Boc-L-Tyr and Gly-NH2/
Characteristics of chymotrypsin modified with water-soluble acylating reagents and its peptide synthesis ability in aqueous organic media.
Kawasaki,Murakami,Dosako,Azuse,Nakamura,Okai
, p. 441 - 444 (2007/10/02)
Several kinds of modified chymotrypsin were prepared with water-soluble acylating reagents, and their characteristics after hydrolyzing with unmodified chymotrypsin in aqueous-N,N'-dimethylformamide (DMF) media were compared. It was found that chymotrypsi
