Líffræðifélag Íslands - biologia.is
Líffræðiráðstefnan 2023

Identification and characterization of xylanases from families GH10 and GH11 sourced from intertidal hot-springs

Höfundar / Authors: Lara Chrystina Malta Neri (1), Hörður Guðmundsson (1), Lilja Björk Jónsdóttir (1), Ólafur H. Friðjónsson (1), Guðmundur Óli Hreggviðsson (1, 2), Björn Þór Aðalsteinsson (1)

Starfsvettvangur / Affiliations: 1. Matís Ohf, 2. University of Iceland

Kynnir / Presenter: Lara Chrystina Malta Neri

Xylan is the second most abundant polysaccharide in nature. Its hydrolysis yields compounds applicable to chemical, food, and pharmaceutical industries. Therefore, bioprospecting for new endo-xylanases is of interest, especially from extreme environments that may yield enzymes applicable in industrial conditions. In this work, twelve endo-xylanases sourced from microbial genomes isolated from intertidal hot-springs were characterized following cloning and expression. Crude enzyme extracts were characterized with the DNS method. Five enzymes displayed optimum catalytic activity at temperatures above 60°C. The optimum pH for the enzymes was at around 5.6-7.0, reflecting their marine origin. The enzymes were generally salt tolerant, or even required salt for catalysis. Seven enzymes had no activity at 0% NaCl. Three enzymes were highly salt tolerant, displaying no loss of activity at 10% NaCl. Taken together, the characterization revealed many candidate enzymes applicable for xylan hydrolysis at elevated temperature and salinity – i.e., at industrially relevant conditions.