| Makale Türü |
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| 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
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| 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 |
| Atıf Sayıları | |
| Web of Science | 7 |
| Scopus | 7 |
| Google Scholar | 10 |
| Dergi Adı | Frontiers in Bioengineering and Biotechnology |
| Kısa Adı | FRONT BIOENG BIOTECH |
| Yayıncı | FRONTIERS MEDIA SA |
| Açık Erişim | Evet |
| ISSN | 2296-4185 |
| E-ISSN | 2296-4185 |
| Wos Quartile | Q1 |
| Scopus Quartile | Q1 |
| Tarandığı Indeksler | SCIE , Scopus |
| WoS Kategoriler | MULTIDISCIPLINARY SCIENCES |
| Scopus Kategoriler | BIOMEDICAL ENGINEERING | BIOTECHNOLOGY | BIOENGINEERING | HISTOLOGY |