NOVELTY - An alkaline protease capable of acting on acidic insulin B-chain and cleaving 26 peptide bonds among 29 peptide bonds of the B-chain and degrading natural proteins e.g. casein and synthetic substrates e.g. N-succinyl-Ala-Ala-Pro-Phe-P-nitroanilide, and having optimum pH of 5-13, optimum temperature of 70degreesC, calcium-independent thermostability, resistance to surfactants e.g. sodium dodecyl sulfate, and molecular weight of 31000-32000, is new.    USE - (V) is useful for producing (I) (claimed). (I) is useful as a protease in detergents, dish washing liquids, washing agents, toilet aromatic agents, water purifying agents, pipe cleaning agents, oligopeptide manufacture, meat softening, leather tanning, and in industries that require degradation of protein, for removing allergens, and for environmental purification.    ADVANTAGE - (I) has high alkali activity, resistance to surfactants and calcium-independent thermostability, and is capable of exhibiting excellent performance in highly alkaline detergents.    DETAILED DESCRIPTION - An alkaline protease (I) having the following physicochemical property: (a) capable of acting on acidic insulin B-chain and cleaving at least 20 peptide bonds (preferably a maximum of 26 peptide bonds) among the 29 peptide bonds of acidic insulin B-chain, (b) substrate specificity: capable of degrading natural proteins such as casein, elastin, keratin, and hemoglobin, and synthetic substrates such as N-succinyl-Ala-Ala-Pro-Phe-P-nitroanilide, N-glutaryl-Ala-Ala-Pro-Leu-p-nitroanilide, N-succinyl-Ala-Ala-Pro-Met-p-nitroanilide, N-methoxy succinyl-Ala-Ile-Pro-Met-p-nitroanilide and N-succinyl-Ala-Ala-Val-Ala-p-nitroanilide, (c) optimum pH: has an optimum pH range of 5-13, preferably around 12.6, and has stable pH range of 5-11 when processed at 50degreesC for 10 minutes, (d) optimum temperature and heat stability: has optimum temperature of 70degreesC and the activity of (I) does not drop by heating upto 65degreesC at pH 10 for 10 minutes, and the thermostability and optimum temperature of (I) are not affected by Ca2+ ions, (e) influence of surface active agent: the activity of (I) is not inhibited by linear alkyl benzene sulfonic acid sodium salt, polyoxyethylene sodium alkylsulfate, sodium dodecyl sulfate (SDS), alpha-olefin sulfonic acid sodium salt, alkane sulfonic acid sodium salt, alpha-sulfo fatty acid ester, and polyoxyethylene alkyl alcohol, and (f) has molecular weight of 31000-32000 as determined by SDS-polyacrylamide gel electrophoresis (PAGE) method.    INDEPENDENT CLAIMS are also included for the following:    (1) an alkaline protease precursor (II) having an amino acid sequence comprising one or more amino acid deletions, substitutions, inversions or insertions in SEQ ID No. 2;    (2) gene (III) encoding (I) or (II) and comprising a polynucleotide chosen from a polynucleotide encoding a polypeptide having amino acid sequence of mature enzyme comprising SEQ ID No. 3, a polynucleotide encoding a polypeptide having an amino acid sequence comprising one or more amino acid deletions, substitutions, inversions or insertions in SEQ ID No. 3, a polynucleotide encoding a polypeptide having SEQ ID No. 2, a polynucleotide encoding a polypeptide having an amino acid sequence comprising one or more amino acid deletions, substitutions, inversions or insertions in SEQ ID No. 2, a polynucleotide having SEQ ID No. 1, and a polynucleotide capable of hybridizing under stringent conditions with polynucleotide having SEQ ID No. 1 and encoding protein having alkaline protease activity;    (3) recombinant vector (IV) comprising (III);    (4) microorganisms (V) transformed with (IV); and    (5) producing (I).    DESCRIPTION OF DRAWING(S) - The figure shows graph representing the relationship between pH and enzymatic activity of the novel alkaline protease. (Drawing includes non-English language text).