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Literature summary for 3.4.22.32 extracted from

  • Mahmood, R.; Saleemuddin, M.
    Additional stabilization of stem bromelain coupled to a thermosensitive polymer by uniform orientation and using polyclonal antibodies (2007), Biochemistry (Moscow), 72, 307-312.
    View publication on PubMed

General Stability

General Stability Organism
Stem bromelain covalently coupled to a thermosensitive polymer of N-isopropylacrylamide either through the amino groups of the enzyme (randomly coupled) or via the lone oligosaccharide chain (uniformly coupled) shows better thermostability. The enzyme coupled via the oligosaccharide chain exhibits better access to the substrate casein as compared to the preparation in which the amino groups formed the point of contact between the enzyme and the polymer. Ananas comosus

Organism

Organism UniProt Comment Textmining
Ananas comosus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
casein + H2O
-
Ananas comosus ?
-
?

Synonyms

Synonyms Comment Organism
Bromelain
-
Ananas comosus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
native enzyme Ananas comosus
60 70 randomly polymer-coupled enzyme preparations Ananas comosus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60
-
native bromelain rapidly loses activity at 60°C and retains only about 10% of the initial activity after incubation for 180 min, about 70% and 58% of the initial activity is retained by uniformly coupled and randomly coupled N-isopropylacrylamide-enzyme preparations, respectively, after 180 min incubation at 60°C Ananas comosus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
native enzyme, at 35°C Ananas comosus
10
-
randomly polymer-coupled enzyme preparations, at 35°C Ananas comosus