Abstract
Twelve bacterial strains were isolated from shrimp paste (Ka-pi) by the standard dilution technique using nutrient broth (NB) medium supplemented with 5% NaCl (w/v). Six rod-shaped isolates were belonged to the genus Bacillus and 6 coccal isolates were Staphylococcus based on their phenotypic characteristics and 16S rRNA gene sequence analyses (98.91–100% sequence similarity). Strain KP1-09 was identified as Bacillus tequilensis, KP1-04 and KP2-03 as B. infantis, KP1-14 as B. flexus, KP2-17 as B. paramycoides and KP1-10 as Bacillus strain. Coccal isolates, KP3-03, KP4-02, KP4-08, KP5-02, KP5-03 and KP5-07 were identified as Staphylococcus cohnii subsp. urealyticus. The lipase activity of strains in modified NB and in modified NB medium supplemented with 1% (v/v) Tween 20 or Tween 80 using para-nitrophenyl butyrate (C4) as a substrate ranged from 4.41±0.17 to 29.68±0.80 Unit/mL. The strain B. flexus KP1-14 cultivated in modified NB medium showed the highest lipase activity. While the strains KP1-10, KP1-09, KP4-02, KP5-02 and KP5-07 cultivated in modified NB medium supplemented with 1% (v/v) Tween 80, showed the lipase activity ranged from 0.32±0.01 to 3.22±0.24 Unit/mL when p-nitrophenyl palmitate (C16) was used as a substrate. The strain S. cohnii subsp. urealyticus KP5-02 showed the highest lipase activity.
Highlights
Lipases (Triacylglycerol acylhydrolase, EC 3.1.1.3) are water soluble enzymes, which catalyze a wide range of reactions, including hydrolysis, interesterification, alcoholysis, acidolysis, esterification, and aminolysis
Six rod-shaped isolates were belonged to the genus Bacillus and six coccal isolates were belonged to the genus Staphylococcus based on their phenotypic characteristics and 16S rRNA gene sequence analyses (98.91%–100% sequence similarity)
The strain B. flexus KP1-14 cultivated in modified nutrient broth (NB) medium showed the highest lipase activity, while the strains KP1-10, KP1-09, KP4-02, KP5-02, and KP5-07 cultivated in modified NB medium supplemented with 1% (v/v) Tween 80 showed the lipase activity ranged from 0.32 ± 0.01 Unit/ml to 3.22 ± 0.24 Unit/ ml when p-nitrophenyl palmitate (C16) was used as a substrate
Summary
Lipases (Triacylglycerol acylhydrolase, EC 3.1.1.3) are water soluble enzymes, which catalyze a wide range of reactions, including hydrolysis, interesterification, alcoholysis, acidolysis, esterification, and aminolysis. These lipases could hydrolyze triacylglycerols to release free fatty acids and glycerol (Javed et al, 2018; Priji et al, 2015). Lipases are ubiquitous in nature and widely distributed in plants, animals, and microorganisms, such as bacteria, yeasts, and fungi. The traditional fermented shrimp paste (Ka-pi), a purplepink to dark brown color, strong odor and paste-like consistency is widely consumed as seasoning ingredient in Thailand. Many microorganisms are found in shrimp paste and their extracellular lipases play a major role in shrimp paste products (Camacho et al, 2009). The aim of this research was to isolate, identify, and screen the lipolytic activity of bacteria from Thai shrimp paste
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
