Endopeptidases extraction

Schneider, G., Sjoling, S., Wallin, E., Wrede, P., Glaser, E., and von Heijne, G. (1998). Feature-extraction from endopeptidase cleavage sites in mitochondrial targeting peptides. Proteins Struct. Fund. Genet. 30, 49-60. 

Deodorization. Volatile flavor components of soybean have been investigated in detail (79, 80, 81, 82). Arai et al. (83) have studied the interaction of denatured soybean protein with 1-hexanol and 1-hexanal which are the typical beany flavor compounds of raw and processed soybeans. These protein-bound compounds are liberated by treating the denatured soybean protein with pepsin (83). Noguchi et al. (84) observed that not only 1-hexanol and 1-hexanal but also other flavor compounds are effectively liberated and removed from a soybean protein isolate during treatment with an acid protease (Molsin). A subsequent study has ascribed this effect to the activity of aspergillopeptidase A, an endopeptidase, which has been identified as a main constituent of Molsin (85). Fujimaki et al. (88, 87) examined several protease preparations for their usefulness in deodorization and reported that a pepsin treatment followed by ether extraction is most effective for deodorizing some protein preparations of soybean and fish. 

Partial proteolysis of soybean proteins with endopeptidases has been used to remove flavor compounds and related fatty materials from soybean curd and defatted soybean flour (21). Certain soybean protein concentrates possess an undesirable beany and oxidized flavor. Treatment of soybean curd and defatted soybean flour with endopeptidases such as aspergillopeptidase A released off-flavor compounds such as 1-hexanal and 1-hexanol which could be removed from the hydrolysate by solvent extraction. The enzymically digested products had less odor, taste, and color than the starting material and were more stable to oxidative deterioration. 

Hemopressin (HP), rHP H-Pro-Val-Asn-Phe-Lys-Phe-Leu-Ser-His-OH, a bioactive 9-peptide derived from the a 1-chain of hemoglobin and initially isolated from rat brain extract. H P has been used as a natural peptide substrate for endopeptidase 24.15, neurolysin, and angiotensin-converting enzyme. The sequence of HP is well... 

Incubation of substrates SEC.1 and AMY.l with brain extracts resulted in extensive i oteolysis by exopeptidases, in addititm to any endopeptidase deavages that nu tove occuned. Th siAstrates woe not en loyM in fiuwr studies of extracts containing ai tidases. 

Documented effects Essential oils from this species are used in the pharmaceutical industry to add an aroma to drugs and in the fragrance industry as an aroma fixative (Khalmatov and Kosimov 1992 Ganunerman et al. 1990). Water and MeOH extracts of the plant strongly inhibited aldose reductase activity, an enzyme associated with diabetic complications (Kasimu et al. 1998). Compounds from the plant were found to inhibit prolyl endopeptidase (PEP), an enzyme thought to be involved with learning and memory processes, and the inhibition of which may produce anti-amnesic effects (Tezuka et al. 1999). 

Tezuka Y, Kasimu R, Li JX, Basnet P, Tanaka K, Namba T, Kadota S (1998) Constituents of roots of Salvia deserta Schemg. (Xinjiemg-Danshen). Chem Pharm Bull 6(1) 107-112 Tezuka Y, Fan W, Kasimu R, Kadota S (1999) Screening of crude drug extracts for prolyl endopeptidase inhibitory activity. Phytomedicine 6(3) 197-203... 

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