Thermostable collagenolytic activity of a novel thermophilic isolate, Bacillus sp. strain NTAP-1

We isolated an acidophilic thermophile belonging to the genus Bacillus, strain NTAP-1, which secreted a thermostable collagenolytic activity into the culture medium. The collagenolytic activity exhibited an optimum pH for Azocoll hydrolysis of pH 3.9 and was not completely inhibited by 10 mM ethylen...

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Veröffentlicht in:Journal of bioscience and bioengineering 2000, Vol.89 (6), p.612-614
Hauptverfasser: Nakayama, Toru, Tsuruoka, Naoki, Akai, Minoru, Nishino, Tokuzo
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container_end_page 614
container_issue 6
container_start_page 612
container_title Journal of bioscience and bioengineering
container_volume 89
creator Nakayama, Toru
Tsuruoka, Naoki
Akai, Minoru
Nishino, Tokuzo
description We isolated an acidophilic thermophile belonging to the genus Bacillus, strain NTAP-1, which secreted a thermostable collagenolytic activity into the culture medium. The collagenolytic activity exhibited an optimum pH for Azocoll hydrolysis of pH 3.9 and was not completely inhibited by 10 mM ethylenediaminetetraacetic acid (residual activity, 63%), suggesting that Bacillus NTAP-1 produces a novel acid proteinase with highest activity for collagen. The collagenolytic activity was thermostable; more than 80% of the original activity was retained after incubation of the culture supernatant at pH 4.0 and 60°C for 4 h.
doi_str_mv 10.1016/S1389-1723(00)80067-5
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source Elsevier ScienceDirect Journals Complete
subjects acidophile
Acids
Bacillus
Bacillus sp
Biodegradation
Biological and medical sciences
Biology of microorganisms of confirmed or potential industrial interest
Biotechnology
Cell culture
Collagen
collagenase
Enzymes
Fundamental and applied biological sciences. Psychology
gelatin
Hydrolysis
Miscellaneous
Mission oriented research
Thermodynamic stability
thermostability
title Thermostable collagenolytic activity of a novel thermophilic isolate, Bacillus sp. strain NTAP-1
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