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Assignment Topic: Bacterial Phytase: Potential Application, in Vivo Function and Regulation of Its Synthesis

Bacterial phytase has potential application as an animal feed additive to enhance the nutritional quality of plant material by liberating phosphate from phytate. Bacterial phytases are inducible enzymes whose expression is subject to complex regulation. Phytase production is turned off in exponentially growing bacteria and starts when cultures enter the stationary phase due to nutrient or energy limitation. Carbon starvation alone can immediately induce phytase synthesis in some bacteria. Phytase is regulated at both the transcriptional and post-transcriptional levels in response to environmental conditions like phosphate availability.

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Iqra Shafique
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0% found this document useful (0 votes)
31 views6 pages

Assignment Topic: Bacterial Phytase: Potential Application, in Vivo Function and Regulation of Its Synthesis

Bacterial phytase has potential application as an animal feed additive to enhance the nutritional quality of plant material by liberating phosphate from phytate. Bacterial phytases are inducible enzymes whose expression is subject to complex regulation. Phytase production is turned off in exponentially growing bacteria and starts when cultures enter the stationary phase due to nutrient or energy limitation. Carbon starvation alone can immediately induce phytase synthesis in some bacteria. Phytase is regulated at both the transcriptional and post-transcriptional levels in response to environmental conditions like phosphate availability.

Uploaded by

Iqra Shafique
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Download as PPTX, PDF, TXT or read online on Scribd
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Assignment topic

Bacterial phytase: potential application, in vivo function


and regulation of its synthesis

Submitted by
Iqra Shafique( roll#1825204017)
Ayesha akram(roll#1825204009)
Submitted to
Dr. Roheena
Subject
Enzymology
MS-I Biotech(2018-20)
Introduction
 These enzymes belong to a special class of
phosphomonoesterases myo-inositol
hexakisphosphate 3-phosphorylase,
 and myo-inositol hexakisphosphate 6-
phosphorylase,

 capable of initiating the stepwise release of


phosphate from phytate [myo-inositol
(1,2,3,4,5,6)
 hexakisphosphate], the major storage form of
phosphate in plant seeds and pollen

 Phytases were originally proposed as an animal


feed additive to enhance the nutritional quality
of plant material in feed for simple-stomached
animals by liberating phosphate.
Occurance
REGULATION OF PHYTASE FORMATION
 phytase is an inducible enzyme and its expression is subjected to
a complex regulation
 phytase production was studied in some detail only in
Escherichia coli and Raoultella terrigena.
 In non-limiting media the formation of both the Escherichia coli
and the Raoultella terrigena phytase was turned off in
exponentially growing bacteria and started as soon as the
cultures entered the stationary phase.
 nutrient or an energy limitation, known to occur in the stationary
phase, could be at the origin of its induction.
 only carbon starvation was able to provoke an immediate
synthesis of the Raoultella terrigena phytase
 Escherichia coli, phytase synthesis was triggered, when bacteria
were starved for inorganic phosphate
Phytase-related factors:
Phytase is a protein molecule that can be digested by endogenous
proteases. Bacterial phytases have greater proteolytic resistence
compared to fungal phytases.

Animal-related factors:
Endogenous phytase activity occurs in the colons of pigs.
Supplementing diets with exogenous phytase shifts phytase
activity to the stomach and upper small intestine. The pH in a
pig’s stomach is 2-2.5 while pH in the crop is 5.2-5.8. This
difference in pH of the main phytase activity sites between species
results in different catalytic efficiencies of the phytase enzyme.

Dietary-related factors:
Phytate level and its interaction with cations and proteins
determines the amount and rate of insoluble mineral-phytate or
protein-mineral-phytate complexes formed.

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