Journal of Pure and Applied MicrobiologyVol. 9 No. 3

Xanthophyllomyces dendrorhous as a New Source of Enzymes and its Enzymatic Potential in Non-Carotenoid Related Applications

A.L. Chew*, F. S. Ang and S.Y. Khaw

Institute For Research In Molecular Medicine (INFORMM), Universiti Sains Malaysia, 11800 USM, Penang, Malaysia.

Received on 11 April 2015 and accepted on 09 June 2015

 

ABSTRACT

Xanthophyllomyces dendrorhous is a red-pigmented, fermentative basidiomycetous yeast which was well documented for the production of astaxanthin for over three decades. Astaxanthin is economically important because it is the most expensive aquaculture feed component for artificial pigmentation of crustaceans, fish and poultry. It also contributes tremendously in human health as it exhibits antioxidant and anti-inflammatory properties. So far, X. dendrorhous has been biotechnologically exploited as a natural source of astaxanthin. Thus, considerable literature has accumulated in the field of astaxanthin production in X. dendrorhous. However, there are no reviews on its enzymatic capabilities. Focus of this review is to examine enzymatic activities that have been briefly reported for X. dendrorhous. The potential applications of these enzymes were also discussed, unveiling the prospective biotechnological use and value of this yeast. These include b-fructofuranosidase for neo-FOS production, a-glucosidase for the production of prebiotic IMOs, b–amylase mainly for starch saccharification, endo-b-1,3(4)-glucanase for the removal of anti-nutritive b-glucan in animal feed, aspartic protease for biocontrol properties against pathogenic fungi and plant diseases and carboxypeptidase for ochratoxin A decontamination. The information presented indicates that besides producing astaxanthin, X. dendrorhous is able to contribute in other aspects especially with its enzymatic capabilities.

Keywords : Xanthophyllomyces dendrorhous, b-fructofuranosidase, a-glucosidase, b–amylase, endo-b-1,3(4)-glucanase, aspartic protease, carboxypeptidase.