Isolation, Screening and Characterization of Yeasts with Amyloytic, Lipolytic, and Proteolytic Activities from the Surface of Philippine Bananas (Musa spp.)


Noel H. Tan Gana1 , Bernadette C. Mendoza2, and Rosario G. Monsalud1

1Philippine National Collection of Microorganisms, National Institute for Molecular Biology and Biotechnology, University of the Philippines Los Baños, College, Los Baños, Laguna, Philippines
2Microbiology Division, Institute of Biological Sciences, College of Arts and Sciences, University of the Philippines Los Baños, College, Los Baños, Laguna, Philippines

corresponding author: This email address is being protected from spambots. You need JavaScript enabled to view it.



Philippine fruits are rarely exploited as microbiological habitats from where yeasts with potential economic benefits can be isolated and identified. In this study, one hundred seventy yeasts were isolated from 5 banana samples. Amylase, lipase, and protease activity were tested on starch agar, Sierra’s medium with tween 80 and casein agar, respectively. Yeasts that tested positive for amylase, lipase, and protease were numbered 29, 76, and 34, respectively. Phenotypic identification of 15 yeasts with moderate to high enzyme activities was done and seven representative strains of the identified species were further subjected to D1/D2 26S ribosomal RNA gene (D1/D2 26S rRNA) sequencing. The yeasts with amylolytic, lipolytic, and/or proteolytic activities were identified as Brandoniozyma complexa, Candida wangnamkhiaoensis, Debaryomyces nepalensis, Hypopichia burtonii, Kodamaea ohmerii, Pichia anomala, Pseudozyma hubeiensis, P. prolifica, and P. pruni.



Microorganisms are a good source of biomolecules such as enzymes, fatty acids, pigments, metabolites and antibiotics, that are of great commercial and industrial importance and this fact has led to the isolation of biotechnologically important microorganisms (Bull 2004). Yeasts for example, have been shown to be good sources of enzymes (Buzzini & Vaughan-Martini 2006). . . . . . . . . . .





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