Aggregate of a peptide‐containing block copolymer with a lipase | Zendy

Naka Kensuke | Zendy; Yamashita Rie | Zendy; Nakamura Tohru | Zendy; Ohki Akira | Zendy; Maeda Shigeru | Zendy; Aoi Keigo | Zendy; Tsutsumiuchi Kaname | Zendy; Okada Masahiko | Zendy

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Aggregate of a peptide‐containing block copolymer with a lipase

Author(s) -

Naka Kensuke,

Yamashita Rie,

Nakamura Tohru,

Ohki Akira,

Maeda Shigeru,

Aoi Keigo,

Tsutsumiuchi Kaname,

Okada Masahiko

Publication year - 1996

Publication title -

macromolecular rapid communications

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.348

H-Index - 154

eISSN - 1521-3927

pISSN - 1022-1336

DOI - 10.1002/marc.1996.030170409

Subject(s) - copolymer , lipase , polymer chemistry , hydrolysis , phenylalanine , chemistry , hydrogen bond , propionate , hydrophobic effect , block (permutation group theory) , chemical engineering , materials science , organic chemistry , polymer , molecule , amino acid , enzyme , biochemistry , geometry , mathematics , engineering

The peptide‐containing block copolymer poly( N ‐acetyliminoethylene)‐ block ‐poly( L ‐phenylalanine) (1) formed large water‐soluble aggregates in water due to the hydrophobic and hydrogen‐bonding character of the poly( L ‐phenylalanine) block. The solution properties of 1 were compared with those of the block copolymer poly( N ‐acetyliminoethylene)‐ block ‐poly( N ‐benzoyliminoethylene) (2) with an analogous structure. 1 formed aggregates even though the poly(phenylalanine) segment was short as compared with 2 in which hydrophobic interaction may be the only driving force to form aggregates. The aggregates have strong capability of incorporating Lipase P and largely increase the hydrolysis activity against p ‐nitrophenyl propionate as compared with that of free Lipase P.

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