| Autor: |
Zheng Zhang, Rui Shi, Xiaoyu Zhu, Lihui Zheng, Mingfei Jin, Deming Jiang, Yelin Wu, Hongliang Gao, Zhongyi Chang, Dongrui Wang, Jiajing Wu, Jing Huang |
| Jazyk: |
angličtina |
| Rok vydání: |
2024 |
| Předmět: |
|
| Zdroj: |
Food Chemistry: X, Vol 22, Iss , Pp 101312- (2024) |
| Druh dokumentu: |
article |
| ISSN: |
2590-1575 |
| DOI: |
10.1016/j.fochx.2024.101312 |
| Popis: |
Protein glutaminase (PG), originating from Chryseobacterium proteolyticum, can catalyze the deamidation of glutamine residues in plant proteins into glutamic acid, thus enhancing its functional properties. However, the low yield of PG limits its industrial production. In this study, the yield of PG in C. proteolyticum TM1040 increased by 121 %, up to 7.30 U/mL in a 15 L fermenter after medium optimization. Subsequently, purified PG was obtained by cation exchange chromatography (CEX) coupled with hydrophobic interaction chromatography (HIC). The degree of deamidation (DD) of wheat gluten after purified PG deamidation was 87.11 %, which is superior to chemical deamidation in safety and DD. The emulsifying and foaming properties of deamidated wheat gluten were 2.67 and 18.86 times higher, and the water- and oil-holding properties were 4.23 and 18.77 times higher, respectively. The deamidated wheat gluten with enhanced functional properties was used to improve the flavor and texture in baking cakes. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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