Effects of Oxygen Transference on Protease Production by Rhodotorula mucilaginosa CBMAI 1528 in a Stirred Tank Bioreactor

Microbial proteases, especially aspartic proteases, are an essential group of enzymes produced from different microorganisms. Microbial proteases have several applications, mainly in the food, beverage, cosmetic, and pharmaceutical industries, due to their efficiency in the processing and in the man...

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Published in:Bioengineering
Main Authors: Suellen Machado, Valker Feitosa, Omar Pillaca-Pullo, Luciana Lario, Lara Sette, Adalberto Pessoa, Harley Alves
Format: Text
Language:English
Published: Multidisciplinary Digital Publishing Institute 2022
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Online Access:https://doi.org/10.3390/bioengineering9110694
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author Suellen Machado
Valker Feitosa
Omar Pillaca-Pullo
Luciana Lario
Lara Sette
Adalberto Pessoa
Harley Alves
author_facet Suellen Machado
Valker Feitosa
Omar Pillaca-Pullo
Luciana Lario
Lara Sette
Adalberto Pessoa
Harley Alves
author_sort Suellen Machado
collection MDPI Open Access Publishing
container_issue 11
container_start_page 694
container_title Bioengineering
container_volume 9
description Microbial proteases, especially aspartic proteases, are an essential group of enzymes produced from different microorganisms. Microbial proteases have several applications, mainly in the food, beverage, cosmetic, and pharmaceutical industries, due to their efficiency in the processing and in the manufacturing stages. The yeast Rhodotorula mucilaginosa CBMAI 1528 was isolated from the Antarctic environment and was previously reported to have higher extracellular aspartic protease production. In addition, advances in the operational conditions of bioreactors for enzyme production are important to reduce the gap associated with scaling−up processes. This is the first study that evaluates the influence of oxygen transference (kLa) on the protease production of R. mucilaginosa yeast. To that end, batch cultures were created in a stirred tank bioreactor using Sabouraud dextrose broth at 25 °C for 72 h under kLa values from 18 to 135 h−1. The results show that kLa (121 h−1) obtained at 500 rpm and 1.5 vvm plays an important role in protease production (124.9 U/mL) and productivity (6.784 U/L.h) as well as biomass (10.4 g/L), μmax (0.14 h−1) and Yx/s (0.484 g/g). In conclusion, R. mucilaginosa showed high yield production in aerobic culture with the efficiency of protease expression and secretion influenced by kLa. In this sense, our results could be used for further industrial investment.
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spelling ftmdpi:oai:mdpi.com:/2306-5354/9/11/694/ 2025-01-16T19:08:48+00:00 Effects of Oxygen Transference on Protease Production by Rhodotorula mucilaginosa CBMAI 1528 in a Stirred Tank Bioreactor Suellen Machado Valker Feitosa Omar Pillaca-Pullo Luciana Lario Lara Sette Adalberto Pessoa Harley Alves agris 2022-11-15 application/pdf https://doi.org/10.3390/bioengineering9110694 EN eng Multidisciplinary Digital Publishing Institute Biochemical Engineering https://dx.doi.org/10.3390/bioengineering9110694 https://creativecommons.org/licenses/by/4.0/ Bioengineering; Volume 9; Issue 11; Pages: 694 extremophilic psychrophilic proteinase proteolytic bioreactor oxygen transference Text 2022 ftmdpi https://doi.org/10.3390/bioengineering9110694 2023-08-01T07:21:30Z Microbial proteases, especially aspartic proteases, are an essential group of enzymes produced from different microorganisms. Microbial proteases have several applications, mainly in the food, beverage, cosmetic, and pharmaceutical industries, due to their efficiency in the processing and in the manufacturing stages. The yeast Rhodotorula mucilaginosa CBMAI 1528 was isolated from the Antarctic environment and was previously reported to have higher extracellular aspartic protease production. In addition, advances in the operational conditions of bioreactors for enzyme production are important to reduce the gap associated with scaling−up processes. This is the first study that evaluates the influence of oxygen transference (kLa) on the protease production of R. mucilaginosa yeast. To that end, batch cultures were created in a stirred tank bioreactor using Sabouraud dextrose broth at 25 °C for 72 h under kLa values from 18 to 135 h−1. The results show that kLa (121 h−1) obtained at 500 rpm and 1.5 vvm plays an important role in protease production (124.9 U/mL) and productivity (6.784 U/L.h) as well as biomass (10.4 g/L), μmax (0.14 h−1) and Yx/s (0.484 g/g). In conclusion, R. mucilaginosa showed high yield production in aerobic culture with the efficiency of protease expression and secretion influenced by kLa. In this sense, our results could be used for further industrial investment. Text Antarc* Antarctic MDPI Open Access Publishing Antarctic The Antarctic Bioengineering 9 11 694
spellingShingle extremophilic
psychrophilic
proteinase
proteolytic
bioreactor
oxygen transference
Suellen Machado
Valker Feitosa
Omar Pillaca-Pullo
Luciana Lario
Lara Sette
Adalberto Pessoa
Harley Alves
Effects of Oxygen Transference on Protease Production by Rhodotorula mucilaginosa CBMAI 1528 in a Stirred Tank Bioreactor
title Effects of Oxygen Transference on Protease Production by Rhodotorula mucilaginosa CBMAI 1528 in a Stirred Tank Bioreactor
title_full Effects of Oxygen Transference on Protease Production by Rhodotorula mucilaginosa CBMAI 1528 in a Stirred Tank Bioreactor
title_fullStr Effects of Oxygen Transference on Protease Production by Rhodotorula mucilaginosa CBMAI 1528 in a Stirred Tank Bioreactor
title_full_unstemmed Effects of Oxygen Transference on Protease Production by Rhodotorula mucilaginosa CBMAI 1528 in a Stirred Tank Bioreactor
title_short Effects of Oxygen Transference on Protease Production by Rhodotorula mucilaginosa CBMAI 1528 in a Stirred Tank Bioreactor
title_sort effects of oxygen transference on protease production by rhodotorula mucilaginosa cbmai 1528 in a stirred tank bioreactor
topic extremophilic
psychrophilic
proteinase
proteolytic
bioreactor
oxygen transference
topic_facet extremophilic
psychrophilic
proteinase
proteolytic
bioreactor
oxygen transference
url https://doi.org/10.3390/bioengineering9110694