دورية أكاديمية
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Amination of naringinase to improve citrus juice debittering using a catalyst immobilized on glyoxyl-agarose.

التفاصيل البيبلوغرافية
العنوان: Amination of naringinase to improve citrus juice debittering using a catalyst immobilized on glyoxyl-agarose.
المؤلفون: Urrutia P; School of Biochemistry Engineering, Pontificia Universidad Católica de Valparaíso, Chile. Electronic address: paulina.urrutia@pucv.cl., Arrieta R; School of Biochemistry Engineering, Pontificia Universidad Católica de Valparaíso, Chile., Torres C; School of Biochemistry Engineering, Pontificia Universidad Católica de Valparaíso, Chile., Guerrero C; School of Biochemistry Engineering, Pontificia Universidad Católica de Valparaíso, Chile., Wilson L; School of Biochemistry Engineering, Pontificia Universidad Católica de Valparaíso, Chile.
المصدر: Food chemistry [Food Chem] 2024 Sep 15; Vol. 452, pp. 139600. Date of Electronic Publication: 2024 May 11.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Elsevier Applied Science Publishers Country of Publication: England NLM ID: 7702639 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1873-7072 (Electronic) Linking ISSN: 03088146 NLM ISO Abbreviation: Food Chem Subsets: MEDLINE
أسماء مطبوعة: Publication: Barking : Elsevier Applied Science Publishers
Original Publication: Barking, Eng., Applied Science Publishers.
مواضيع طبية MeSH: Fruit and Vegetable Juices*/analysis , Enzymes, Immobilized*/chemistry , Enzymes, Immobilized*/metabolism , Sepharose*/chemistry , Glyoxylates*/chemistry, Amination ; Hydrogen-Ion Concentration ; Citrus/chemistry ; Citrus/enzymology ; Enzyme Stability ; Biocatalysis ; Multienzyme Complexes/chemistry ; Multienzyme Complexes/metabolism ; Glycoside Hydrolases/chemistry ; Glycoside Hydrolases/metabolism ; beta-Glucosidase/chemistry ; beta-Glucosidase/metabolism ; Temperature ; Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Flavanones/chemistry ; Flavanones/metabolism ; Catalysis
مستخلص: A naringinase complex was chemically aminated prior to its immobilization on glyoxyl-agarose to develop a robust biocatalyst for juice debittering. The effects of amination on the optimal pH and temperature, thermal stability, and debittering performance were analyzed. Concentration of amino groups on catalysts surface increased in 36 %. Amination reduced the β-glucosidase activity of naringinase complex; however, did not affect optimal pH and temperature of the enzyme and it favored immobilization, obtaining α-l-rhamnosidase and β-d-glucosidase activities of 1.7 and 4.2 times the values obtained when the unmodified enzymes were immobilized. Amination favored the stability of the immobilized biocatalyst, retaining 100 % of both activities after 190 h at 30 °C and pH 3, while its non-aminated counterpart retained 80 and 52 % of α-rhamnosidase and β-glucosidase activities, respectively. The immobilized catalyst showed a better performance in grapefruit juice debittering, obtaining a naringin conversion of 7 times the value obtained with the non-aminated catalyst.
Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2024 Elsevier Ltd. All rights reserved.)
فهرسة مساهمة: Keywords: Chemical amination; Enzyme; Grapefruit juice; Immobilization; Naringin
المشرفين على المادة: EC 3.2.1.- (naringinase)
0 (Enzymes, Immobilized)
105054-62-4 (glyoxyl agarose)
9012-36-6 (Sepharose)
0 (Glyoxylates)
0 (Multienzyme Complexes)
EC 3.2.1.- (Glycoside Hydrolases)
EC 3.2.1.21 (beta-Glucosidase)
0 (Bacterial Proteins)
0 (Flavanones)
تواريخ الأحداث: Date Created: 20240514 Date Completed: 20240530 Latest Revision: 20240530
رمز التحديث: 20240531
DOI: 10.1016/j.foodchem.2024.139600
PMID: 38744138
قاعدة البيانات: MEDLINE
الوصف
تدمد:1873-7072
DOI:10.1016/j.foodchem.2024.139600