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hydrophobic residues (peptides half dozen to 9) with a large aspect chain e.g., leucine, essential amino acid, essential amino acid and essential amino acid. However, if the organic compound contributory the group of the bond was aromatic the bond was not hydrolysed although the C-terminal amino acid was deliquescent. Neither L-Trp-Gly nor L-Tyr-Gly was hydrolysed. It seems that the presence of a deliquescent organic compound at the N-terminal finish is not needed for the

Nil Z-Gly-Onp 1.63 5.29 10 Unbranched Z-L-Ala-Onp 3.27 16.94 320.00 Branched Z-L-Val-ONP 16.30 0.48 9.07

Aromatic Z-L-phe-Onp 3.27 1.02 09.28

Imino acid Z-L-pro-Onp 163.00 0.0 0.0

(E0)(M) V0/E0

Z-L-Leu-Onp 3.27 2.14 10.45 Z-L-lleu-Onp 16.30 0.21 3.97

Z-L-Tyr-Onp 3.27 1.69 31.94 Z-L-Trp-Onp 3.27 0.74 13.99

Moles/sec/mole enzyme

163.00 0.0 0.0

% Relative activity\*

In Table 3, the results of the speed measurements given for 10 parts as Vo/Eo wherever Vo is initial rate and Eo is concentration of the protein in moles. The concentration of substrate used was one.56 10-4 M. If the metric linear unit values of the p-nitrophenyl esters of CBZ-amino acids were of constant magnitude as for different thiol proteases like papain [9], ficin [17], bromelain [18] and ananain [12] then Vo/Eo values obtained for Glycine and amino acid were love the

The refined solanain of Vallaris family Solanaceae showed close to identical

Substrate specificity studies showed solanain exhibited broad specificity. It showed peptidase activity, amidase activity. The enzyme was capable of catalysing the hydrolysis of p-nitrophenyl esters of amino acids. It exhibited difference in

Solanain, differs from the amino alkanoic acid proteases in having low amidase activity with BAPNA and conjointly did not show any esterase activity with BAEE. This finding suggests considerably low specificity for essential amino acid residues. It differs from enzyme, ficin and bromelain during this facet. By showing broad specificity, Solanain resembled enzyme [11], ficin [14, 17] and bromelain [18] that change a spread of amide bonds. All these, however, showed a preference for basic amino acids. The solanain of Vallaris potato family hydrolysed leucyl bonds with efficiency and during this respect resembled ficin [17] and differed from bromelain

Kcat values of the corresponding esters of different proteases.

specificity towards all the substrates.

Substrate 108

N,N1 -di-Z-L Lys-Onp

Hydrolysis of various synthetic ester substrates with purified solanain.

\*Calculated taking activity toward Z-Gly-ONp as 100%.

Amino acid side chain p-Nitrophenyl ester

Peptide Synthesis

specificity towards simple peptide substrates.

protein.

Table 4.

[18] (Table 4).

12. Conclusion

76

Silpa Somavarapu Department of Food Technology, Vikrama Simhapuri University, Nellore, Andhra Pradesh, India

\*Address all correspondence to: silpasomavarapu.1981@gmail.com

© 2019 The Author(s). Licensee IntechOpen. This chapter is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/ by/3.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
