Optimization of Hemoglobin Chitosan Glycosylation Conditions and Structural Characteristics and Functions of Glycosylated Hemoglobin after an <i>In vitro</i> Digestion

Zhan, Junqi; Li, Gaoshang; Tan, Beibei

doi:10.1080/10498850.2021.1946231

Cited by 8 publications

(6 citation statements)

References 27 publications

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“…Therefore, whether the TGase-type protein glycation induced an alteration in protein bioactivities aroused extensive attention in the past years. It was observed that the chitosan-glycation of hemoglobin by TGase resulted in respective 11.06% and 30.49% increases in anti-oxidant activity and iron bioavailability [ 41 ], while the glucosamine-glycation of bovine β-lactoglobulin by TGase led to a weakened allergic reactivity including a reduced IgG/IgE binding capacity [ 4 ]. More importantly, the previous results from our groups also indicated that oligochitosan-glycation of casein by TGase brought about higher barrier protection for the casein hydrolysates in IEC-6 cells [ 6 , 33 ].…”

Section: Discussionmentioning

confidence: 99%

Casein Oligochitosan-Glycation by Transglutaminase Enhances the Anti-Inflammatory Potential of Casein Hydrolysates to the Lipopolysaccharide-Stimulated IEC-6 Cells

et al. 2022

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In this study, milk protein casein was glycated by oligochitosan through the catalysis of transglutaminase (TGase) and then hydrolyzed by trypsin. The obtained glycated casein hydrolysates (GCNH) were assessed for their anti-inflammatory activities, using the lipopolysaccharide (LPS)-stimulated rat intestinal epithelial cells (IEC-6) as cell models and the casein hydrolysates (CNH) without TGase catalysis as controls. The results showed that GCNH had oligochitosan incorporation and thus possessed a glucosamine content of 5.74 g/kg protein. In general, GCNH at dose levels of 25–100 μg/mL could elevate IEC-6 cell growth, and at dose levels of 25–50 μg/mL, they were also able to alleviate the LPS-induced cytotoxicity by increasing cell viability efficiently. Although LPS caused clear inflammation in the LPS-stimulated cells, GCNH were capable of reducing the secretion of three pro-inflammatory mediators including interleukin-1β (IL-1β), IL-6, and tumor necrosis factor-α, or promoting the secretion of two anti-inflammatory mediators like IL-10 and transforming growth factor-β, demonstrating their anti-inflammatory activities to the stimulated cells. Moreover, GCNH also could down-regulate the expression of three inflammation-related proteins including TLR4, p-p38, and p-p65 in the stimulated cells, and thus possessed a capacity to suppress the phosphorylation of p38 and p65 proteins as well as to inactivate the NF-κB and MAPK signaling pathways. Additionally, a higher GCNH dose level consistently led to higher anti-inflammatory effect in the cells, while GCNH were always more potent than CNH at performing anti-inflammatory function targets. It is thus suggested that the TGase-catalyzed casein oligochitosan-glycation could enhance the anti-inflammatory activities of casein hydrolysates efficiently. TGase-catalyzed protein glycation thus might enhance the healthcare function of protein ingredients in the body.

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Section: Discussionmentioning

confidence: 99%

Casein Oligochitosan-Glycation by Transglutaminase Enhances the Anti-Inflammatory Potential of Casein Hydrolysates to the Lipopolysaccharide-Stimulated IEC-6 Cells

et al. 2022

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“…Infrared spectroscopy and secondary structure analysis was carried out according the method of Zhan et al (2021) with some modification. Samples accompanied with KBr were subjected to FTIR analysis using a spectrometer (Bruker vertex70, Coventry, Germany).…”

Section: Ftir Analysismentioning

confidence: 99%

“…Hydrophobic amino acids play an important role in scavenging free radicals (Samaranayaka & Li-Chan, 2011). It is reported that the antioxidant properties of peptides were related to the presence of hydrophobic amino acids (Zhan et al, 2021), and hydrophobic amino acids are also related to the ACE inhibitory activity in structure-activity relationship (Yang et al, 2020).…”

Section: Amino Acid Analysismentioning

confidence: 99%

Functional properties, structural characteristics and biological activities of deer blood hydrolysates obtained by using different protease

Chang

HUANG

et al. 2022

Food Sci. Technol

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Fresh sika deer blood obtained by Shilu Co., Ltd, Changchun which had passed quarantine inspection and removed fibrous protein by stirring with a stick to avoid coagulation, then diluted two times with deionized water. The mixture was submerged in ice, then disrupted with ultrasound for 5 s by a 3 s interval for 15 min at the power of 500 watts. Enzymatic hydrolysis of deer bloodEnzyme, including pepsin (1:3000, CAS: 9001-75-6), trysin (250 U/mg, CAS: 9002-07-7) and alacase (200 U/mg, CAS: 9014-01-1) were purchased from Shanghai yuanye Bio-Technology Co., Ltd, Shanghai. The preparation of hydrolysates were according the method of the report (Zheng et al., 2019) with some modification. Specifically, the hydrolysis with pepsin (DBH-P) (enzyme/substrate ratio, 2%) was conducted at 40 o C and pH 2.0, trysin treatment (DBH-T) (enzyme/

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“…Compared with glycosylation proteins of monosaccharides, disaccharides and oligosaccharides, polysaccharide glycosylation proteins exhibit better functional properties. Glycosylation has been a hot topic in protein modification research, as it has been found to improve the functional properties of glycosylated haemoglobin (Zhan et al ., 2021; Sun et al ., 2022a), whey protein isolate (WPI) (Wang & Ismail, 2012; Dai et al ., 2018; Guo et al ., 2018; Wang et al ., 2020a; Li et al ., 2022; Yu‐Tong et al ., 2022), rice protein (Cheng et al ., 2017, 2021), pea protein isolate (Kutzli et al ., 2020), bovine serum albumin (Kim & Shin, 2016; Nasrollahzadeh et al ., 2017), rapeseed protein isolate (Qu et al ., 2018a, 2018b), soy protein isolate (Jiang & Zhao, 2011; Yao & Zhao, 2015; Dong et al ., 2023; Feng et al ., 2023; Zhang et al ., 2023b), myosin fibre protein (Jian et al ., 2016; Liu et al ., 2017; Gao et al ., 2018, 2022; Duan et al ., 2023), casein (Bi et al ., 2016; Yousefi et al ., 2017; Zhao et al ., 2021; Kong et al ., 2023; Zhang et al ., 2023a), myosin (Yuan et al ., 2017; Ahmed et al ., 2018), and lactoferrin (Dyer et al ., 2016; Li et al ., 2020; Chen et al ., 2021; Wang et al ., 2022b, 2023) to varying degrees in terms of solubility, emulsifying ability, foaming ability, thermal stability, gelling ability, antioxidant activity, and antibacterial activity.…”

Section: Introductionmentioning

confidence: 99%

Recent advances, challenges and functional applications of protein glycosylation modification in food industry

Hu,

Wang,

Zeng

et al. 2024

Int J of Food Sci Tech

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SummaryProtein glycosylation modification is an effective way to enhance the functional properties of natural proteins. This study aims to explore the preparation of glycosylation products (PPCs) through the Maillard reaction or enzymatic glycosylation using transglutaminase. The study discusses the advantages and disadvantages of preparing PPCs using dry heat, wet heat, and enzymatic glycosylation, as well as factors influencing the glycosylation process. Compared to natural proteins, PPCs demonstrate superior functional properties, including solubility, viscosity, emulsifying ability, gelling ability, thermal stability, antioxidant activity, and antibacterial activity. With improved functional performance, PPCs have broad application prospects as raw materials in food processing. For example, PPCs can be used as antioxidants, emulsifiers, gelling agents, and carriers for various bioactive molecules in the food industry. In the pharmaceutical field, PPCs are expected to serve as contrast agents and dressings. Furthermore, the application of PPCs in food processing should also consider specific processing requirements to achieve the intended enhancement of glycosylated protein functionality.

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Optimization of Hemoglobin Chitosan Glycosylation Conditions and Structural Characteristics and Functions of Glycosylated Hemoglobin after an In vitro Digestion

Cited by 8 publications

References 27 publications

Casein Oligochitosan-Glycation by Transglutaminase Enhances the Anti-Inflammatory Potential of Casein Hydrolysates to the Lipopolysaccharide-Stimulated IEC-6 Cells

Casein Oligochitosan-Glycation by Transglutaminase Enhances the Anti-Inflammatory Potential of Casein Hydrolysates to the Lipopolysaccharide-Stimulated IEC-6 Cells

Functional properties, structural characteristics and biological activities of deer blood hydrolysates obtained by using different protease

Recent advances, challenges and functional applications of protein glycosylation modification in food industry

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