R
Rosamma Philip
Researcher at Cochin University of Science and Technology
Publications - 144
Citations - 2772
Rosamma Philip is an academic researcher from Cochin University of Science and Technology. The author has contributed to research in topics: Penaeus monodon & Antimicrobial peptides. The author has an hindex of 28, co-authored 136 publications receiving 2291 citations.
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Marine yeast Candida aquaetextoris S527 as a potential immunostimulant in black tiger shrimp Penaeus monodon.
TL;DR: It is demonstrated that marine yeast diet administered once every seven days conferred better protection to P. monodon against WSSV infection, supported by the hematological and immune gene expression profiles analyzed.
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Activated packed bed bioreactor for rapid nitrification in brackish water hatchery systems
TL;DR: The packed bed bioreactor shall enable hatchery systems to operate under closed recirculating mode and pave the way for better water management in the aquaculture industry.
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Optimization of carbon and nitrogen sources and growth factors for the production of an aquaculture probiotic (Pseudomonas MCCB 103) using response surface methodology
TL;DR: A new medium for enhanced production of biomass of an aquaculture probiotic Pseudomonas MCCB 103 and its antagonistic phenazine compound, pyocyanin is developed.
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Vibrios associated with Macrobrachium rosenbergii (De Man, 1879) larvae from three hatcheries on the Indian southwest coast
TL;DR: The diversity of Vibrio species associated with Macrobrachium rosenbergii larvae and their virulence characteristics based on haemolysis in prawn blood agar is reported, suggesting that antibiotic application may not be of much use to protect the larvae from vibriosis.
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A marine bacterium, Micrococcus MCCB 104, antagonistic to vibrios in prawn larval rearing systems
N. S. Jayaprakash,S. Somnath Pai,Abdulaziz Anas,R. Preetha,Rosamma Philip,I. S. Bright Singh +5 more
TL;DR: Micrococcus MCCB 104 was demonstrated to be non-pathogenic to M. rosenbergii larvae and the antagonistic component of the extracellular product was heat-stable and insensitive to proteases, lipase, catalase and alpha-amylase.