Loading…
Cold active pectinase, amylase and protease production by yeast isolates obtained from environmental samples
The present study was performed to screen for psychrophilic yeasts that are able to secrete cold active enzymes. Yeast isolates were obtained from environmental samples from northern Turkey and examined for enzyme production at low temperatures. The isolates which were capable of cold active enzyme...
Saved in:
Published in: | Extremophiles : life under extreme conditions 2018-07, Vol.22 (4), p.599-606 |
---|---|
Main Authors: | , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Summary: | The present study was performed to screen for psychrophilic yeasts that are able to secrete cold active enzymes. Yeast isolates were obtained from environmental samples from northern Turkey and examined for enzyme production at low temperatures. The isolates which were capable of cold active enzyme production on plates were identified by molecular identification techniques. It has been found that the isolates belonged to three genera of yeasts, i.e.,
Rhodosporidiobolus
,
Cystofilobasidium
and
Yamadazyma.
The isolates were then fermented in different media at 15 °C and the pectinase, amylase and protease activities were determined in the range of 0.76–1.73, 0.5–1.57 and 2.11–10.53 U/mL, respectively. Maximum enzyme activities were found in
Yamadazyma
isolates for all three enzymes. To the best of our knowledge, cold active pectinase, amylase and protease production by
Yamadazyma
spp. were investigated for the first time in the present study. Besides, this is the first report which indicates cold active amylase production by
Cystofilobasidium capitatum
and pectinase production by
Rhodosporidiobolus colostri.
Yeast isolates obtained in this study may have potential for industrial cold active enzyme production. |
---|---|
ISSN: | 1431-0651 1433-4909 |
DOI: | 10.1007/s00792-018-1020-0 |