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Helvellisin, a novel alkaline protease from the wild ascomycete mushroom Helvella lacunosa

Paper ID Volume ID Publish Year Pages File Format Full-Text
21535 43227 2010 5 PDF Available
Title
Helvellisin, a novel alkaline protease from the wild ascomycete mushroom Helvella lacunosa
Abstract

A 33.5-kDa serine protease designated as helvellisin was isolated from dried fruiting bodies of the wild ascomycete mushroom Helvella lacunosa. It was purified by using a procedure which entailed ion exchange chromatography on DEAE-cellulose, CM-Sepharose, Q-Sepharose, and FPLC-gel filtration on Superdex 75. The protease was characterized by unique N-terminal amino acid sequence, thermostability and pH stability. The protease exhibited a pH optimum of 11.0 and a temperature optimum of 65 °C, with about 40% activity remaining at 87 °C and pH 5 and 13. Helvellisin demonstrated a protease activity of 14 600 U/mg toward casein. The Km of the purified protease for casein was 3.81 mg/ml at pH 11.0 and 37 °C. The Vmax was 5.35 × 10− 2 mg ml− 1 min− 1. It was adversely affected by phenylmethylsulfonyl fluoride, suggesting that it is serine protease. The activity of the protease was enhanced by Mg2+, Fe2+ and Mn2+, but was curtailed by Cu2+, Hg2+ and Fe3+. It was devoid of antifungal and ribonuclease activities.

Keywords
Mushroom; Alkaline protease; Helvella lacunosa; Purification; Characterization; Fruiting bodies
First Page Preview
Helvellisin, a novel alkaline protease from the wild ascomycete mushroom Helvella lacunosa
Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 109, Issue 1, January 2010, Pages 20–24
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering