CN-114432406-B - Application of barley germ vinegar in prolonging life of insects

Abstract

The invention discloses an application of barley germ vinegar in prolonging life of insects. The method can be specifically applied to the preparation of products for prolonging the service life of nematodes by using barley embryo vinegar. The invention discovers that the barley germ vinegar can play a role in prolonging the service life of the caenorhabditis elegans, can be used for preparing related products, and has good market prospect.

Inventors

• MA HONGRUI
• WU SHUANG
• Huang Dailei
• MA LAN
• LI MING
• Ren futian
• YANG GUANG

Assignees

• 北京南苓生物科技有限公司

Dates

Publication Date

20260512

Application Date

20220304

Claims (1)

1. 1. The application of the barley germ vinegar preparation in preparing products for prolonging the service life of caenorhabditis elegans is characterized in that the preparation process of the barley germ vinegar preparation comprises the steps of adding barley germs into mature vinegar with total acidity of more than 6%, refluxing for 3 hours at 100 ℃, repeating three times of extraction, filtering to obtain supernatant, and removing vinegar by adopting a vacuum rotary steaming mode.

Description

Application of barley germ vinegar in prolonging life of insects Technical Field The invention belongs to the field of application of bioactive extracts, and particularly relates to application of barley germ vinegar in prolonging life of insects. Background Ubiquitin is a polypeptide containing 76 amino acids, which is present in many different tissues and organs other than bacteria, and has the effect of labeling proteins to be degraded. Ubiquitin-tagged proteins are degraded in the proteasome. The ubiquitin-controlled protein degradation has important physiological significance, can remove wrong proteins, and has important regulation and control effects on cell growth cycle, DNA replication and chromosome structure. The active center of the proteasome degradation protein is located in the center of the barrel structure and isolated from other parts of the cell. The only access to the active site is a "lock" (a 19S complex) which recognizes the ubiquitinated protein, breaks its folded structure and assists the protein in passing through the narrow channel of the proteasome into the active site at the center of the barrel structure. After the protein is degraded into short peptide fragments of 7 to 9 amino acids in length, it is released from the other segment of the proteasome. In addition, the 19S complex contains an isopeptidase which is capable of removing ubiquitin from the substrate protein. Thus, the proteasome itself is not selective for the protein, and the selective is the E3 enzyme, which ubiquitinates only the protein to be degraded. Ubiquitination regulation plays an important role in the course of cellular life. The ubiquitin-proteasome degradation pathway is the most main protein degradation pathway in eukaryotic cells, and participates in various physiological processes, including at least transcriptional regulation, cell cycle, apoptosis, DNA damage repair, metabolism, immunity and the like. In transcriptional regulation, some transcriptional regulators such as nuclear factor kB (NF-kB), cell cycle important regulator (E2F), protooncogene products c-Fos and c-jun, etc. can be used as substrates to be regulated by ubiquitin-proteasome pathway to activate or inactivate downstream gene expression. In the regulation of apoptosis, studies have found that some apoptosis-related regulatory molecules such as Bcl-2 and srp60 are degraded by ubiquitin-proteasome. In the regulation of the cell cycle, the normal operation of the cell cycle is regulated by various cyclin (cyclin) and cell cycle dependent kinases CDK and CDK inhibitors. It was found that ubiquitin-proteasomes modulate CDK and CDK inhibitor activity, and CDK inhibitor p27 and cyclin D, cyclin E, etc. are important substrates for ubiquitin proteasomes. In immunization, the ubiquitin-proteasome pathway is an essential link for presentation of major histocompatibility complex-restricted class I antigens (MHC-I). Endogenous proteins in antigen presenting cells are degraded by the 26S proteasome into polypeptides and transported to the cell membrane surface in association with MHC class I molecules in the endoplasmic reticulum for recognition by cytotoxic T cells. Ubiquitin-proteinase system (UPS) is a high-selectivity protein degradation system dependent on ATP existing in eukaryotic cells, and has the functions of eliminating aging, injury and misfolded proteins. It is involved in regulating a variety of important biological functions such as inflammation, immune response, cellular senescence, signal transduction, etc. The abnormality can cause disorder of intracellular homeostasis, resulting in various diseases such as tumor, neurodegenerative diseases, cardiovascular diseases, kidney diseases, etc. Ubiquitination level is closely related to cell metabolism and aging. Aging has been reported to result in decreased ubiquitination levels in nematodes, leading to hindered protein recognition and degradation processes. When protein clearance is accelerated using gene knockout therapy, nematode aging conditions are improved and the average life span can be prolonged by 21% at maximum. In liver diseases, ubiquitin-proteasomes are associated with alcoholic liver disease and viral hepatitis. Studies have shown that core proteins in hepatitis C cannot degrade due to the binding of mono-ubiquitin or seldom-ubiquitin, resulting in disease development. Early inflammatory bowel disease (VEOIBD) is a severe form of Inflammatory Bowel Disease (IBD), which occurs in infants under 6 years of age. Recently, studies have found that after mutation of the inflammatory corpuscle NLRP3, the combination of the inflammatory corpuscle NLRP3 with intestinal highly expressed deubiquitinase BRCC3 and JOSD is promoted to promote the deubiquitination of the NLRP3, thereby promoting the activation of the inflammatory corpuscle NLRP3 and finally causing VEOIBD to occur. Cardiomyopathy is the main lethal cause of duchenne muscular dystrophy, the typical pathology of which