Human AlkB homolog H5 (ALKBH5) is a primary m6A demethylase, which is dysregulated and acts as a biological and pharmacological role in human cancers or non-cancers. ALKBH5 plays a dual role in various cancers through regulating kinds of biological processes, such as proliferation, migration, invasion, metastasis and tumor growth. In addition, it takes a great part in human non-cancer, including reproductive system diseases. The underlying regulatory mechanisms of ALKBH5 that relys on m6A-dependent modification are implicated with long non-coding RNA, cancer stem cell, autophagy and hypoxia. ALKBH5 is also an independent prognostic indicator in various cancers. In this review, we summarized the current evidence on ALKBH5 in diverse human cancers or non-cancers and its potential as a prognostic target.

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Chicken egg white (CEW) is a perfect source of natural proteins that possesses outstanding functional properties and various bioactivities. The glycosylation structure of CEW proteins plays important roles in their functions, bioactivities, and allergies. The present work attempted to identify N-glycosites of CEW proteins using an omics strategy. CEW proteins were digested with trypsin and chymotrypsin; glycopeptides were enriched and deglycosylated using PNGase F in HO water, followed by analysis using high-performance liquid chromatography/tandem mass spectrometry (HPLC-MS/MS). A total of 71 N-glycosites in 26 CEW glycoproteins were identified. Web-Logo analysis showed that most of the N-glycosites were at N-X-T (55%) and N-X-S (32%). Furthermore, two-dimensional electrophoresis of CEW clusterin demonstrated a series of spots horizontally distributed at 35-37 kDa with an extremely wide isoelectric point range of 4.54-6.68, indicating the heterogeneity of glycosylation of CEW clusterin. These results provided important information for the understanding of the structures, functions, and bioactivities of CEW glycoproteins.

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The study investigated the volatile compounds of sesame oil and the effects of microwave processing (0–8 min with 1‐min intervals), mainly focusing on the integral flavor characteristics and individual aroma‐active compounds. A total of 82 characteristic odors were identified using GC×GC‐TOF/MS. Fifteen volatile compounds with the highest odor activity values (OAV > 100) were selected as the key odors contributing to the flavor profile of microwaved sesame oil, including 2‐methyl‐propanal (pungent, malt, green), 2‐methyl‐butanal (cocoa, almond), furaneol (caramel), 1‐octen‐3‐one (mushroom), 4‐methyl‐3‐penten‐2‐one (sweet), 1‐nonanol (fat, citrus, green), 2‐methyl‐phenol (phenol), 2‐methoxy‐phenol (smoke, sweet), 2‐methoxy‐4‐vinylphenol (clove, curry), 2,5‐dimethyl‐pyrazine (cocoa, roasted nut, roast beef), 2‐furfurylthiol (coffee, roast), 2‐thiophenemethanethiol (sulfur), methanethiol (gasoline, garlic), methional (cooked potato), and dimethyl trisulfide (fish, cabbage). The OAVs significantly increased with a longer microwave process. Meanwhile, PCA results based on E‐nose and cluster analysis results based on GC×GC‐TOF/MS were similar to distinguish flavor formation during the microwave process. Practical applications Sesame oils were prepared by a microwave process. Aroma‐active compounds with the highest OAVs in sesame oils were not clear. Identification of key aroma compounds of sesame oils could adopt a comprehensive assessment method in combination with E‐nose and individual odors detection. Microwave pretreatment as a new processing technology for sesame oil extraction could reduce the time consumption and produce a unique fragrant flavor compared to the traditional roasting process.

Posttranslational N-glycosylation of food proteins plays a critical role in their structure and function. However, the N-glycoproteome of chicken egg yolk (CEY) has not been studied yet. Glycopeptides hydrolyzed from CEY proteins were enriched, with deglycosylation occurring using PNGase F, and then were identified using a shotgun glycoproteomics strategy. A total of 217 N-glycosylation sites and 86 glycoproteins were identified in CEY, and these glycoproteins are mainly involved in the binding, biological regulation, catalytic activity, and metabolic processes. Among the identified CEY glycoproteins, 22 were recognized as proteases and protease inhibitors, suggesting that a proteinase/inhibitor regulation system exists in CEY; further, 15 were members of the complement and immune systems, which provide protection against potential threats during hatching.The study provides important structural information about CEY glycoproteins and aids in the understanding of the underlying mechanism of embryo development as well as changes in CEY functional characteristics during storage and processing.