TECHNOLOGY FOCUS - BIOTECHNOLOGY - Preferred Sequence: In (I) amino acids are added, deleted or substituted. SPECIFIC SEQUENCES - The protein in (I) consists of the amino acids sequence, (A) and (B):    (i) Ala-Ser-Gly-Ser-Ala-Thr-Gly-His-Lys-Met Thr-Asn-Phe-Ala-Gln-lle-Tyr-Asn-Ala-Gly (A); and    (ii) Thr-Ser-Gly-Thr-Thr-Trp-Thr-Asn-Glu-Thr-Val-Trp-Asn-Asn-Leu-Asn-Glu-Asn-Gly-Ala-Thr- Gly-Gly-Ser-Pro-Ser-Thr Phe-Glu-Pro-Gln-Pro-Ser-Trp-Gln-Asn-Gly-Val-Gly-Gln (B).    The microorganism which produces carboxyl protease MB8 is Chi-proteobacteria, named as Chi-proteobacteria Sp. MB8 of a specific strain, FERMP-16948.    EXAMPLE - SPYN medium (pH 4.5) containing soluble starch (1%), peptone (0.1%), yeast extract (0.1%), nutrient broth (0.05%), potassium nitrate (0.2%), sodium chloride (0.2%), magnesium sulphate (0.005%), calcium chloride (0.002%) and ferrous sulphate (0.001%) was used for performing aerobic culture (at 30 degrees Centigrade). The strain that used SPYN agar medium, isolated (1-7 days), streak cultured, purified. The strain having protease activity was isolated using the parameter that strain having the activity cultivated on ACS agar medium produced a zona pellucida (halo) on the periphery of a colony. The microorganism was isolated, purified, assayed for enzyme activity and Chi-proteobacteria Sp.MB8 strain was selected purified by gel filtration and chromatography and evaluated for its enzymological properties. For evaluating pH stability of carboxyl protease MB8 (I), (I) was added to Clark-Lubs buffer (pH 1-2) and Mcllvaine buffer (pH 2-8) and left for 12 hours at 4 degrees Centigrade. A 10 minute enzyme reaction was performed using haemoglobin and residual activity was measured. Results showed that (I) was stable at pH 3.5-5.5. Molecular weight was found to be 61,000 +/- 1,000 by SDS-PAGE. Sensitivity opposing to pepstatin which was the specific inhibitor of carboxyl protease was evaluated. I (10 mug/ml) was added with Mcllvaine buffer and pepstatin was added at 37 degrees Centigrade with haemoglobin as substrate. After 10 minutes reaction residual activity was measured. Results showed that (I) was not inhibited by pepstatin.