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AbstractExploring the untapped potential of deep-sea microorganisms, particularly their cold-active enzymes, or psychrozymes, offers exciting possibilities for revolutionizing various aspects of the food processing industry. This review focuses on these enzymes, derived from the largely unexplored depths of the deep ocean, where microorganisms have developed unique adaptations to extreme conditions. Psychrozymes, as bioactive molecules, hold significant promise for food industry applications. However, despite their potential, the understanding and industrial utilization of psychrozymes remains limited. This review provides an in-depth analysis of how psychrozymes can: improve processing efficiency, enhance sensory qualities, extend product shelf life, and reduce energy consumption across the food production chain. We explore the cryodefense strategies and cold-adaptation mechanisms that support these enzymes, shedding light on the most extensively studied psychrozymes and assessing their journey from theoretical applications to practical use in food production. The key properties, such as stability, substrate specificity, and catalytic efficiency in cold environments, are also discussed. Although psychrozymes show considerable promise, their large-scale application in the food industry remains largely unexplored. This review emphasizes the need for further research to unlock the full potential of psychrozymes, encouraging their broader integration into the food sector to contribute to more sustainable food production processes. [ABSTRACT FROM AUTHOR]

Fungi, which are widely distributed across the Earth, have successfully managed to colonize cold environments (e.g., polar regions, alpine ecosystems, and glaciers) despite the challenging conditions for life. They are capable of living in extremely harsh environments due to their ecological versatility and morphological plasticity. It is also believed that lower eukaryotes are the most adapted to life at low temperatures among microorganisms that thrive in cold environments. They play important ecological roles, contributing to nutrient recycling and organic matter mineralization. These highly specialized microorganisms have developed adaptation strategies to overcome the direct and indirect harmful influences of low temperatures. They have evolved a wide range of complex and cooperative adaptations at various cellular levels, including modifications to the cell envelope and enzymes, the production of cryoprotectants and chaperones, and the development of new metabolic functions. Adaptation to cold environments has made fungi an exciting source for the discovery of new cold-adapted enzymes (e.g., proteinases, lipases) and secondary metabolites (e.g., pigments, osmolytes, polyunsaturated fatty acids) for widespread use in biotechnology, food technology, agriculture, pharmaceutics, molecular biology, textile industry, and environmental bioremediation in cold climates. This review aims to provide a comprehensive overview of the adaptive strategies employed by psychrophilic yeasts and fungi, highlighting their ecological roles and biotechnological potential. Understanding these adaptive mechanisms not only sheds light on microbial life in extreme environments but also paves the way for innovative applications in the food industry and agriculture. [ABSTRACT FROM AUTHOR]

Fungi, which are widely distributed across the Earth, have successfully managed to colonize cold environments (e.g., polar regions, alpine ecosystems, and glaciers) despite the challenging conditions for life. They are capable of living in extremely harsh environments due to their ecological versatility and morphological plasticity. It is also believed that lower eukaryotes are the most adapted to life at low temperatures among microorganisms that thrive in cold environments. They play important ecological roles, contributing to nutrient recycling and organic matter mineralization. These highly specialized microorganisms have developed adaptation strategies to overcome the direct and indirect harmful influences of low temperatures. They have evolved a wide range of complex and cooperative adaptations at various cellular levels, including modifications to the cell envelope and enzymes, the production of cryoprotectants and chaperones, and the development of new metabolic functions. Adaptation to cold environments has made fungi an exciting source for the discovery of new cold-adapted enzymes (e.g., proteinases, lipases) and secondary metabolites (e.g., pigments, osmolytes, polyunsaturated fatty acids) for widespread use in biotechnology, food technology, agriculture, pharmaceutics, molecular biology, textile industry, and environmental bioremediation in cold climates. This review aims to provide a comprehensive overview of the adaptive strategies employed by psychrophilic yeasts and fungi, highlighting their ecological roles and biotechnological potential. Understanding these adaptive mechanisms not only sheds light on microbial life in extreme environments but also paves the way for innovative applications in the food industry and agriculture.

Antarctica serves as an ideal prototype to study past climatic condition as the ice core records dates back to 100,000 years. Microbiological research on ice core has opened a doorway to our understanding on biodiversity and its contribution to the frozen ecosystem. In this review, the ice core bacterial diversity of East and West Antarctica has been documented. Cold-adapted bacteria hold immense potential in biotechnological applications as they possess functional advantages over mesophilic bacteria. Some of the neoteric applications of bioproducts of Antarctic bacteria have been stated in this review. The current climate change due to global warming exerts a humongous effect on the ecosystem of the polar region. The region being susceptible to any fluctuation in temperature, the exacerbated melting of Antarctic glaciated mass contributes to the rise of global sea level, with loss of ice harbouring unknown microbial entities. This review mainly focuses on the bacterial diversity of East and West Antarctic counterparts, the prevalence of antibiotic-resistant genes, the adaption strategies conferred by bacteria thriving in Antarctic habitats and their potential biotechnological applications. [ABSTRACT FROM AUTHOR]

The bulk of Earth’s biosphere is cold (

The bulk of Earth's biosphere is cold (<5 °C) and inhabited by psychrophiles. Biocatalysts from psychrophilic organisms (psychrozymes) have attracted attention because of their application in the ongoing efforts to decrease energy consumption. Proteinases as a class represent the largest category of industrial enzymes. There has been an emphasis on employing cold-active proteases in detergents because this allows laundry operations at ambient temperatures. Proteases have been used in environmental bioremediation, food industry and molecular biology. In view of the present limited understanding and availability of cold-active proteases with diverse characteristics, it is essential to explore Earth's surface more in search of an ideal cold-active protease. The understanding of molecular and mechanistic details of these proteases will open up new avenues to tailor proteases with the desired properties. A detailed account of the developments in the production and applications of cold-active proteases is presented in this review. [ABSTRACT FROM AUTHOR]

The cold active β-galactosidase from psychrophilic bacteria accelerate the possibility of outperforming the current commercial β-galactosidase production from mesophilic sources. The present study is carried out to screen and isolate a cold active β-galactosidase producing bacterium from profound marine waters of Bay-of-Bengal and to optimize the factors for lactose hydrolysis in milk. Isolated bacterium 3SC-21 was characterized as marine psychrotolerant, halophile, gram negative, rod shaped strain producing an intracellular cold active β-galactosidase enzyme. Further, based upon the 16S rRNA gene sequence, bacterium 3SC-21 was identified as Thalassospira sp. The isolated strain Thalassospira sp. 3SC-21 had shown the enzyme activity between 4 and 20 °C at pH of 6.5 and the enzyme was completely inactivated at 45 °C. The statistical method, central composite rotatable design of response surface methodology was employed to optimize the hydrolysis of lactose and to reveal the interactions between various factors behind this hydrolysis. It was found that maximum of 80.18 % of lactose in 8 ml of raw milk was hydrolysed at pH of 6.5 at 20 °C in comparison to 40 % of lactose hydrolysis at 40 °C, suggesting that the cold active β-galactosidase from Thalassospira sp. 3SC-21would be best suited for manufacturing the lactose free dairy products at low temperature. [ABSTRACT FROM AUTHOR]

Enzymes from psychrophiles catalyze the reactions at low temperatures with higher specific activity. Among all the psychrophilic enzymes produced, cold active β-galactosidase from marine psychrophiles revalorizes a new arena in numerous areas at industrial level. The hydrolysis of lactose in to glucose and galactose by cold active β-galactosidase offers a new promising approach in removal of lactose from milk to overcome the problem of lactose intolerance. Herein we propose, a 3D structure of cold active β-galactosidase enzyme sourced from Pseudoalteromonas haloplanktis by using Modeler 9v8 and best model was developed having 88% of favourable region in ramachandran plot. Modelling was followed by docking studies with the help of Auto dock 4.0 against the three substrates lactose, ONPG and PNPG. In addition, comparative docking studies were also performed for the 3D model of psychrophilic β-galactosidase with mesophilic and thermophilic enzymes. Docking studies revealed that binding affinity of enzyme towards the three different substrates is more for psychrophilic enzyme when compared with mesophilic and thermophilic enzymes. It indicates that the enzyme has high specific activity at low temperature when compared with mesophilic and thermophilic enzymes.