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SUNFLOWER PROTEIN ENZYMATIC HYDROLYSIS AND PLANT PEPTONE PRODUCTION AS A SOURCE OF NITROGEN FOR NUTRIENT MEDIA

Dmitry V. Baurin

First published: 2019-06-20https://doi.org/10.5593/sgem2019/6.1/s25.121View metrics

Abstract

Industrially defatted non-dehulled sunflower meal (SFM) with a protein content 22%, fibre 38% and cellulose 23% was separated into several fractions: protein fraction and lignocellulosic fraction, then they can be used for bioconversion into value added products. The protein concentrate (PC) contained 83% of protein. Hydrolysis of this concentrate by the commercial proteases, such as Proteinase T, Protex 7L, Protex 40E (Danisco Genecor, Denmark) and Pancreatin (Biosynthesis, the Russian Federation) can transform this concentrate into protein hydrolysate with higher content of amine nitrogen. Amino nitrogen content for different enzymatic preparations varied from 1.5 to 2.8 mg per ml and was significantly higher when combination of preparations was used. Composition and high solubility of sunflower hydrolysates at wide range of pH values proved that the product had potential for sunflower peptone production and its use as a nitrogen source for nutrient media. Crude protein was determined by the Kjeldahl method. Amine nitrogen was measured by Sorensen method (formaline titration method). Several bacterial strains were chosen as test objects and they proved to accumulate a significant amount of biomass with high cell count per ml.

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Publication details

Title
SUNFLOWER PROTEIN ENZYMATIC HYDROLYSIS AND PLANT PEPTONE PRODUCTION AS A SOURCE OF NITROGEN FOR NUTRIENT MEDIA
Authors
Dmitry V. Baurin
Proceedings
SGEM International Multidisciplinary Scientific GeoConference EXPO Proceedings; 19th International Multidisciplinary Scientific GeoConference SGEM2019, Nano, Bio, Green and Space: Technologies for Sustainable Future
Publisher
STEF92 Technology
Year
2019
Pages
939-946
SWS Citekey
Baurin201925939946
ISSN
1314-2704
ISBN
978-619-7408-88-1
Language
en
Publication type
Conference Paper
Keywords
References14
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