Abstract
White-gourd protease was rapidly inactivated by methylene blue catalysed photooxidation at pH 8.0 and 200.The rate of inactivation was pH-dependent and became slower at lower pH values, suggesting the involvement of some histidine residues in the inactivation.Changes in the amino acid composition occurred only with histidine residues.One mole or more of histidine residues in the molecule are essential importance in the catalytic function of white-gourd protease.
Abstract from the paper’s OpenAlex record; open copy licensed cc-by-nc-nd. Read at the source ↗
The text the model read, with the source record’s inline markup (italics, sub- and superscripts) rendered and its character entities decoded; quote offsets refer to the raw text.
Claims 4
Claim · model-written summary
Methylene blue photooxidation rapidly inactivated white-gourd protease.
- Taxon
- White-gourde0
- Treatment
- methylene blue catalysed photooxidatione0
- Outcome
- proteasee0
- Direction
- inactivatede0
- Qualifier
- pH 8.0 and 200e0
Not reportedComparator
Verbatim
e0“White-gourd protease was rapidly inactivated by methylene blue catalysed photooxidation at pH 8.0 and 200.”
Claim · model-written summary
Inactivation was slower at lower pH.
Verbatim
e0“The rate of inactivation was pH-dependent and became slower at lower pH values”
t0“トウガン”
Claim · model-written summary
Only histidine residues changed in amino acid composition.
Verbatim
e0“Changes in the amino acid composition occurred only with histidine residues.”
t0“トウガン”
Claim · model-written summary
At least one mole of histidine residues is essential for white-gourd protease catalytic function.
Verbatim
e0“One mole or more of histidine residues in the molecule are essential importance in the catalytic function of white-gourd protease.”