Proteases from alkaliphilic or alkalitolerant bacteria isolated from Manleluag hyperalkaline spring in Pangasinan

Date

2021

Abstract

Protease is an enzyme that hydrolyzes peptide bonds of proteins and breaks them down into polypeptides or free amino acids. This study was conducted to assess protease activities of 106 alkaliphilic bacteria isolated from water, microbial mat, and sediment samples from Manleluag Hyperalkaline Spring by Skim Milk Assay. Thirty-five isolates showed protease activity and were ranked according to their Cz values. The five isolates with the highest protease activities as suggested by the lowest Cz values were SNE 3 (Cz 0.2908), SNE 2 (Cz 0.2971), SNE 9 (Cz 0.3338), W10 (Cz 0.3426), and W1 (Cz 0.3611). Molecular identification based on 16S rDNA showed closest similarities of the five isolates with Bacillus pseudofirmus OF4 (99% similarities; SNE 3 and SNE 2), Cellulosimicrobium funkei W6122 (99% similarity; SNE 9), and Bacillus hornekiae 1P01SC (96% similarities; W10 and W1). Proteolytic activities of the enzymes for each isolates were determined by in-solution digestion using bovine serum albumin (BSA) and zymography using gelatin and casein as substrate. The presence of gelatinases and caseinases as revealed by clearing bands with proteolytic activities, suggests the molecular weights of the proteases in kDa present in the alkaliphilic or alkalitolerant isolates.

Language

English

Document Type

Article

Pages /Collation

41 leaves

En – AGROVOC descriptors

SPRING; PROTEASES; PROTEINASE INHIBITORS; ENZYMES; FREE AMINO ACIDS; ALKALINITY; NUCLEOTIDE SEQUENCE; WATER PURIFICATION

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