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Kinetics of α‐amylase secretion in Aspergillus oryzae
Author(s) -
Henriksen Anne L. Santerre,
Carlsen Morten,
de Bang Henriette,
Nielsen Jens
Publication year - 1999
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/(sici)1097-0290(19991005)65:1<76::aid-bit9>3.0.co;2-d
Subject(s) - aspergillus oryzae , secretion , kinetics , penicillium chrysogenum , amylase , glycosylation , secretory protein , methionine , biology , biochemistry , intracellular , chemistry , biophysics , enzyme , amino acid , physics , quantum mechanics
Pulse and pulse‐chase experiments have been performed to study L‐[ 35 S] methionine incorporation and protein secretion kinetics in Aspergillus oryzae. Pulse experiments confirmed the mechanism of methionine uptake reported previously for Penicillium chrysogenum (Benko et al., 1967). Pulse‐chase experiments were carried out to investigate the α‐amylase secretion kinetics in A. oryzae. No unglycosylated α‐amylase was detected neither intracellularly nor extracellularly demonstrating that glycosylation was not the rate controlling step in the secretory pathway. The pulse chase experiments indicated that there are two pools of intracellular α‐amylase: a fast secreted and a slow secreted. The secretion of those two pools were described with a kinetic model, which was fitted to the pulse chase experiments. © 1999 John Wiley & Sons, Inc. Biotechnol Bioeng 65: 76–82, 1999.