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Stabilization of a supplemental digestive enzyme by post-translational engineering using chemically-activated polyethylene glycol.

Abstract：

:Many enzymes used as digestive aids exhibit, at best, moderate stability when incubated under gastrointestinal conditions. A supplemental β-galactosidase administered orally to treat lactose intolerance was conjugated to 40 kDa, branched polyethylene glycol (PEG). PEGylation increased the enzyme's relative activity at lower pH values (2.5-4.5) and doubled enzyme stability at pH 2.5. The PEGylated enzyme retained significantly more residual activity after exposure to simulated gastric conditions (52% versus 31%), a consequence of protection from both pepsin and low pH mediated inactivation. Conjugation also provided significant protection against the proteolytic component of pancreatin. Overall, the PEGylated enzyme retained over twice the levels of residual activity recorded for non-PEGylated enzyme after exposure to complete simulated gastrointestinal conditions. PEGylation also marginally improved the enzyme's kinetic characteristics. When using its physiological substrate (lactose), K(m) values recorded were slightly decreased (from 83 to 60 μM) and k(cat)/K(m) values (M(-1) s(-1)) were increased from 100 to 147. This appears to be the first report of the use of a conjugated PEG to stabilize a digestive enzyme and the first report of the ability of conjugated PEG to stabilize a protein at low pH.

journal_name

Biotechnol Lett

journal_title

Biotechnology letters

authors

Turner KM,Pasut G,Veronese FM,Boyce A,Walsh G

doi

10.1007/s10529-010-0474-7

subject

Has Abstract

pub_date

2011-03-01 00:00:00

pages

617-21

issue

3

eissn

0141-5492

issn

1573-6776

journal_volume

33

pub_type

杂志文章

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