↓ Skip to main content

Purification and properties of an alkaline protease from alkalophilic Bacillus sp. KSM-K16

Overview of attention for article published in Applied Microbiology and Biotechnology, July 1995
Altmetric Badge

Mentioned by

wikipedia
2 Wikipedia pages

Citations

dimensions_citation
98 Dimensions

Readers on

mendeley
40 Mendeley
Title
Purification and properties of an alkaline protease from alkalophilic Bacillus sp. KSM-K16
Published in
Applied Microbiology and Biotechnology, July 1995
DOI 10.1007/bf00218452
Pubmed ID
Authors

T. Kobayashi, Y. Hakamada, S. Adachi, J. Hitomi, T. Yoshimatsu, K. Koike, S. Kawai, S. Ito

Abstract

Alkaline protease (EC 3.4.21.14) activity, suitable for use in detergents, was detected in the alkaline culture medium of Bacillus sp. KSM-K16, which was originally isolated from soil. The enzyme, designated M protease, was purified to homogeneity from the culture broth by column chromatographies. The N-terminal amino acid sequence was Ala-Gln-Ser-Val-Pro-Trp-Gly-Ile-Ser-Arg- Val-Gln-Ala-Pro-Ala-Ala-His-Asn-Arg-Gly-Leu-Thr-Gly. The molecular mass of the protease was 28 kDa, and its isoelectric point was close to pH 10.6. Maximum activity toward casein was observed at 55 degrees C and at pH 12.3 in 50 mM phosphate/NaOH buffer. The activity was inhibited by phenylmethylsulfonyl fluoride and chymostatin. The enzyme was very stable in long-term incubation with liquid detergents at 40 degrees C. The enzyme cleaved the oxidized insulin B chain initially at Leu15-Tyr16 and efficiently at ten more sites. Among various oligopeptidyl p-nitro-anilides (pNA) tested, N-succinyl-Ala-Ala-Pro-Phe-pNA was efficiently hydrolyzed by M protease. M protease was precipitated in (NH4)2SO4-saturated acetate buffer (pH 5.0) as plank-like crystals.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 40 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Mexico 1 3%
Unknown 39 98%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 11 28%
Researcher 5 13%
Student > Master 4 10%
Student > Bachelor 4 10%
Other 3 8%
Other 2 5%
Unknown 11 28%
Readers by discipline Count As %
Agricultural and Biological Sciences 11 28%
Biochemistry, Genetics and Molecular Biology 8 20%
Engineering 2 5%
Chemistry 2 5%
Unspecified 1 3%
Other 3 8%
Unknown 13 33%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 3. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 23 September 2009.
All research outputs
#8,022,830
of 24,119,703 outputs
Outputs from Applied Microbiology and Biotechnology
#2,748
of 8,034 outputs
Outputs of similar age
#7,596
of 24,744 outputs
Outputs of similar age from Applied Microbiology and Biotechnology
#8
of 22 outputs
Altmetric has tracked 24,119,703 research outputs across all sources so far. This one is in the 44th percentile – i.e., 44% of other outputs scored the same or lower than it.
So far Altmetric has tracked 8,034 research outputs from this source. They receive a mean Attention Score of 4.3. This one is in the 36th percentile – i.e., 36% of its peers scored the same or lower than it.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 24,744 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 8th percentile – i.e., 8% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 22 others from the same source and published within six weeks on either side of this one. This one is in the 1st percentile – i.e., 1% of its contemporaries scored the same or lower than it.