Formation and Properties of Horseradish Peroxidase Colloidal Clusters

✍ Scribed by Alexander Kamyshny; Tali Reuveni; Shlomo Magdassi

• Publisher: Elsevier Science
• Year: 1996
• Tongue: English
• Weight: 322 KB
• Volume: 181
• Category: Article
• ISSN: 0021-9797
• DOI: 10.1006/jcis.1996.0404

✦ Synopsis

ene glycol (14), and 2,4-bis(O-methoxypolyethylene glycol)-Hydrophobic modification of horseradish peroxidase by fatty 6-chloro-S-triazine (16).

acid esters (C 8 , C 12 , C 16 , C 18 ) of N-hydroxysuccinimide was car-However, so far there have been no reports on the modifiried out. The degree of modification increases with an increase in cation of HRP by long-chain hydrophobic groups. This type the ester:enzyme molar ratio and reaches a maximal value of four of modification may alter its surface activity and could also modified amino groups when this ratio is 150:1. Covalent attachlead to unique applications in the field of biosensors, which ment of hydrophobic groups to the peroxidase molecules leads to are currently under investigation. Such modifications were a spontaneous formation of micelle-like colloidal clusters, which carried out by us for various proteins, and it was found that have a mean diameter of 65 nm at the maximal degree of modifisuch covalent binding of long hydrophobic chains to a procation by C 16 -ester. The fraction of the enzyme molecules which forms clusters depends on both the length of the attached hy-tein molecule could result in the formation of surface-active drophobic chain and the degree of modification. The colloidal proteins and even in the formation of colloidal micelle-like clusters, which are composed of the modified peroxidase, have structures (17-20).

about 80 and 50% lower enzymatic activities for C 12 -and C 16 -

The purpose of this research was to investigate the possimodified enzymes.