Immobilization of a Bifidobacterial Endo-ß-N-Acetylglucosaminidase to Generate Bioactive Compounds for Food Industry
 
Yazarlar (11)
Öğr. Gör. Burcu Pekdemir Çanakkale Onsekiz Mart Üniversitesi, Türkiye
Arş. Gör. Hatice Duman Çanakkale Onsekiz Mart Üniversitesi, Türkiye
Ayşenur Arslan Çanakkale Onsekiz Mart Üniversitesi, Türkiye
Merve Kaplan Çanakkale Onsekiz Mart Üniversitesi, Türkiye
Melda Karyelioğlu Çanakkale Onsekiz Mart Üniversitesi, Türkiye
Tolgahan Özer Çanakkale Onsekiz Mart Üniversitesi, Türkiye
Doç. Dr. Hacı Mehmet KAYILI Karabük Üniversitesi, Türkiye
Prof. Dr. Bekir Salih Hacettepe Üniversitesi, Türkiye
Bethany M. Henrick University Of Nebraska–Lincoln, Amerika Birleşik Devletleri
Rebbeca M. Duar
Evolve Biosystems Inc., Amerika Birleşik Devletleri
Prof. Dr. Sercan Karav Çanakkale Onsekiz Mart Üniversitesi, Türkiye
Makale Türü Açık Erişim Özgün Makale (SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale)
Dergi Adı Frontiers in Bioengineering and Biotechnology (Q1)
Dergi ISSN 2296-4185 Dergi Bilgileri (2022)
Dergi Tarandığı Indeksler SCI-Expanded
Makale Dili İngilizce Basım Tarihi 07-2022
Cilt / Sayı / Sayfa 10 / 1 / 1–10 DOI 10.3389/fbioe.2022.922423
Makale Linki https://www.frontiersin.org/articles/10.3389/fbioe.2022.922423/full
UAK Araştırma Alanları
Biyoteknoloji
Özet
Conjugated N-glycans are considered next-generation bioactive prebiotic compounds due to their selective stimulation of beneficial microbes. These compounds are glycosidically attached to proteins through N-acetylglucosamines via specific asparagine residue (AsN-X-Ser/Thr). Certain bacteria such as Bifidobacterium longum subspecies infantis (B. infantis) have been shown to be capable of utilizing conjugated N-glycans, owing to their specialized genomic abilities. B. infantis possess a unique enzyme, Endo-ß-N-acetylglucosaminidase (EndoBI-1), which cleaves all types of conjugated N-glycans from glycoproteins. In this study, recombinantly cloned EndoBI-1 enzyme activity was investigated using various immobilization methods: 1) adsorption, 2) entrapment-based alginate immobilization, 3) SulfoLink-, and 4) AminoLink-based covalent bonding immobilization techniques were compared to develop the optimum application of EndoBI-1 to food processes. The yield of enzyme immobilization and the activity of each immobilized enzyme by different approaches were investigated. The N-glycans released from lactoperoxidase (LPO) using different immobilized enzyme forms were characterized using MALDI-TOF mass spectrometry (MS). As expected, regardless of the techniques, the enzyme activity decreased after the immobilization methods. The enzyme activity of adsorption and entrapment-based alginate immobilization was found to be 71.55% ± 0.6 and 20.32% ± 3.18, respectively, whereas the activity of AminoLink- and SulfoLink-based covalent bonding immobilization was found to be 58.05 ± 1.98 and 47.49% ± 0.30 compared to the …
Anahtar Kelimeler
B. infantis | bioactive compounds | Endo-ß-N-acetylglucosaminidase | immobilization | N-glycans
BM Sürdürülebilir Kalkınma Amaçları
Atıf Sayıları
Web of Science 7
Scopus 7
Google Scholar 10
Immobilization of a Bifidobacterial Endo-ß-N-Acetylglucosaminidase to Generate Bioactive Compounds for Food Industry

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