Rennin - 9001-98-3

Rennin

Catalog Number: EVT-3567933
CAS Number: 9001-98-3
Molecular Formula: C30H27N3O15
Molecular Weight: 669.5 g/mol
The product is for non-human research only. Not for therapeutic or veterinary use.
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Product Introduction

Description
Rennin, also known as chymosin, is a proteolytic enzyme primarily found in the gastric mucosa of ruminant animals. It plays a crucial role in the digestion of milk proteins, specifically casein, by catalyzing the hydrolysis of peptide bonds. Rennin has garnered significant attention due to its potential applications in various fields, including medical, environmental, and industrial research. This paper aims to provide an overview of the synthesis/extraction methods, chemical structure, biological activity, biological effects, applications, and future perspectives of rennin.
Applications in Various Fields
, and Future Perspectives

Properties

CAS Number

9001-98-3

Product Name

Rennin

IUPAC Name

N-[(3S,7S,11S)-7,11-bis[(2,3-dihydroxybenzoyl)amino]-2,6,10-trioxo-1,5,9-trioxacyclododec-3-yl]-2,3-dihydroxybenzamide

Molecular Formula

C30H27N3O15

Molecular Weight

669.5 g/mol

InChI

InChI=1S/C30H27N3O15/c34-19-7-1-4-13(22(19)37)25(40)31-16-10-46-29(44)18(33-27(42)15-6-3-9-21(36)24(15)39)12-48-30(45)17(11-47-28(16)43)32-26(41)14-5-2-8-20(35)23(14)38/h1-9,16-18,34-39H,10-12H2,(H,31,40)(H,32,41)(H,33,42)/t16-,17-,18-/m0/s1

InChI Key

SERBHKJMVBATSJ-BZSNNMDCSA-N

SMILES

C1C(C(=O)OCC(C(=O)OCC(C(=O)O1)NC(=O)C2=C(C(=CC=C2)O)O)NC(=O)C3=C(C(=CC=C3)O)O)NC(=O)C4=C(C(=CC=C4)O)O

Canonical SMILES

C1C(C(=O)OCC(C(=O)OCC(C(=O)O1)NC(=O)C2=C(C(=CC=C2)O)O)NC(=O)C3=C(C(=CC=C3)O)O)NC(=O)C4=C(C(=CC=C4)O)O

Isomeric SMILES

C1[C@@H](C(=O)OC[C@@H](C(=O)OC[C@@H](C(=O)O1)NC(=O)C2=C(C(=CC=C2)O)O)NC(=O)C3=C(C(=CC=C3)O)O)NC(=O)C4=C(C(=CC=C4)O)O
Method of Synthesis or Extraction
Rennin can be synthesized or extracted using different methods. The most common methods include microbial fermentation, recombinant DNA technology, and extraction from animal sources. Microbial fermentation involves the cultivation of microorganisms, such as fungi or bacteria, that naturally produce rennin. Recombinant DNA technology allows for the production of rennin by genetically modifying microorganisms or using host cells to express the rennin gene. Extraction from animal sources involves isolating rennin from the gastric mucosa of young ruminant animals.
The efficiency and yield of each method vary. Microbial fermentation and recombinant DNA technology offer higher yields and better control over the production process. However, extraction from animal sources remains a viable option for obtaining rennin, especially in regions where animal by-products are readily available. Environmental and safety considerations are crucial in rennin production. Microbial fermentation and recombinant DNA technology have minimal environmental impact and reduce the need for animal sources, thus promoting sustainability. Additionally, these methods ensure the absence of potential contaminants and allergens associated with animal-derived rennin.
Chemical Structure and Biological Activity
Rennin is a protease enzyme belonging to the aspartic protease family. It consists of two identical subunits, each containing approximately 323 amino acids. The active site of rennin contains two catalytic aspartic acid residues, which play a crucial role in its proteolytic activity.
The mechanism of action of rennin involves the specific cleavage of the kappa-casein protein, resulting in the formation of a soluble calcium-sensitive casein fraction called para-kappa-casein. This cleavage leads to the coagulation of milk, facilitating the digestion of milk proteins in the stomach.
Rennin exhibits high specificity towards its biological targets, primarily acting on casein proteins. Its potency is attributed to its ability to selectively hydrolyze peptide bonds at specific sites within the casein molecule.
Biological Effects
Rennin's biological effects extend beyond its role in milk digestion. It has been found to influence cell function and signal transduction pathways. Rennin has been implicated in the regulation of blood pressure, as it can generate angiotensin peptides involved in vasoconstriction. Additionally, rennin has been associated with the modulation of immune responses and the regulation of cell growth and differentiation.
The potential therapeutic effects of rennin have been explored in various medical research areas. It has shown promise in drug development, particularly in the formulation of novel therapeutics for hypertension and cardiovascular diseases. Clinical trials have demonstrated rennin's efficacy in reducing blood pressure and improving cardiovascular health. However, potential side effects, such as hyperkalemia and gastrointestinal disturbances, need to be carefully monitored.
In environmental research, rennin's effects on ecosystems and its role in pollution management have been investigated. Rennin has been utilized in wastewater treatment processes to degrade organic pollutants, demonstrating its potential in sustainable pollution management. However, further research is needed to assess its environmental impact and optimize its application in different ecosystems.
In industrial research, rennin finds applications in manufacturing processes, particularly in the dairy industry. It is used to coagulate milk during cheese production, improving product quality and efficiency. Health and safety considerations are essential in industrial applications to ensure the absence of contaminants and allergens in the final products.
Future Perspectives and Challenges
Despite the potential of rennin, several limitations hinder its widespread use and study. The availability of rennin from animal sources may be limited, and ethical concerns regarding animal welfare may arise. Additionally, the cost and scalability of rennin production using microbial fermentation or recombinant DNA technology need to be optimized for commercial viability.
Possible solutions and improvements include the development of more efficient rennin production processes, such as using alternative host cells or optimizing fermentation conditions. Advances in protein engineering and enzyme modification techniques may also enhance rennin's stability, specificity, and catalytic efficiency.
Future trends and prospects in the application of rennin in scientific research include exploring its potential in targeted drug delivery systems, investigating its role in cancer therapy, and further understanding its impact on the gut microbiome. Additionally, the integration of rennin in sustainable biotechnological processes, such as biofuel production or waste management, holds promise for addressing environmental challenges.
In conclusion, rennin is a proteolytic enzyme with diverse applications in medical, environmental, and industrial research. Its synthesis/extraction methods, chemical structure, biological activity, and effects on cell function and signal transduction have been explored. Rennin's potential therapeutic and toxic effects, as well as its applications in medical, environmental, and industrial research, have been discussed. Despite current limitations, future perspectives and challenges offer opportunities for further advancements and applications of rennin in scientific research.

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