Preprint Article Version 1 Preserved in Portico This version is not peer-reviewed

Production Optimization, Partial Characterization, and Gluten-Digesting Ability of the Acid Protease from Clavispora lusitaniae PC3

Scheherazed Dakhmouche Djekrif
* ORCID logo ,
Amel Ait Kaki El Hadef El Okki
,
Leila Bennamoun
,
Abdelhak Djekrif
,
Tahar Nouadri
,
Louisa Gillmann
Version 1 : Received: 5 January 2024 / Approved: 8 January 2024 / Online: 8 January 2024 (13:47:54 CET)

A peer-reviewed article of this Preprint also exists.

Djekrif, S.D.; El Hadef El Okki, A.A.K.; Bennamoun, L.; Djekrif, A.; Nouadri, T.; Gillmann, L. Production Optimization, Partial Characterization, and Gluten-Digesting Ability of the Acidic Protease from Clavispora lusitaniae PC3. Fermentation 2024, 10, 139. Djekrif, S.D.; El Hadef El Okki, A.A.K.; Bennamoun, L.; Djekrif, A.; Nouadri, T.; Gillmann, L. Production Optimization, Partial Characterization, and Gluten-Digesting Ability of the Acidic Protease from Clavispora lusitaniae PC3. Fermentation 2024, 10, 139.

Abstract

: Protease-producing yeasts were isolated from potato wastes and screened for protease production on skim milk agar plates The best producer of protease isolate was identified as Clavispora lusitaniae. The strain showed better enzyme production using tomato pomace and bread waste mix as a solid fermentation substrate. The optimized conditions improved enzyme activity and showed a maximal production of 33450±503 IU/g compared with the initial activity of 11205,78 ±360 without medium optimization. A threefold increase in protease activity after medium optimization proved the reliability of using the PBD and CCD design. A 19.76-fold purified enzyme and a yield of 32.94% were obtained after purification. The protease showed maximum activity at pH 4 and 60 °C and was resistant to Tween 20, Tween 40, SDS, and β-mercaptoethanol, Ca2+, and Mg2+ stimulated it. The protease activity was strongly inhibited in the presence of urea, and EDTA. The results revealed Clavispora lusitaniae protease's ability to degrade wheat seeds and flour gluten by 98.7% and 97% respectively under pH 4 for 24 hours at 40 °C. According to this study, this enzyme could be a potential candidate for the food industry, particularly for treating wheat seed and flour to reduce the immunogenicity of gluten.

Keywords

Clavispora lusitaniae PC3; protease; solid- state fermentation; enzyme purification; gluten degradation

Subject

Biology and Life Sciences, Biology and Biotechnology

Copyright: This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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