Enzymes play vital roles in all organisms. The enzymatic process is progressively at its peak, mainly for producing biochemical products with a higher value. The immobilization of enzymes can sometimes tremendously improve the outcome of biocatalytic processes, making the product(s) relatively pure and economical. Carrier-free immobilized enzymes can increase the yield of the product and the stability of the enzyme in biocatalysis. Immobilized enzymes are easier to purify. Due to these varied advantages, researchers are tempted to explore carrier-free methods used for the immobilization of enzymes. In this review article, we have discussed various aspects of enzyme immobilization, approaches followed to design a process used for immobilization of an enzyme and the advantages and disadvantages of various common processes used for enzyme immobilization.

The incidence of cancer continues to increase worldwide, resulting in significant physical, emotional, and financial challenges for individuals, families, communities, and healthcare systems. Cancer is projected to be responsible for approximately 10 million deaths in 2020, accounting for one in six deaths globally. Prostate, colon, lung, and breast cancers are the most common types of cancer. In India, it is estimated that there will be around 2.7 million cancer patients by 2020. Personalized medicine has the potential to offer an alternative approach to cancer treatment. Precision medicine, often known as personalized medicine, is a new cancer treatment technique that focuses on tailoring medication to each patient's specific genetic, biochemical, and lifestyle factors. The goal is to optimize tumor response while minimizing therapy side effects, resulting in improved patient care and quality of life. Personalized medicine allows for the creation of focused medicines that address specific gene mutations by leveraging knowledge about a patient's cancer, including its genetic makeup. Ongoing research seeks to detect gene modifications in diverse cancer types, produce novel diagnostic tools, and develop treatments that particularly target these genetic changes. In recent years, personalized medicine has achieved major advances in the treatment of solid tumors, with the promise to improve treatment precision, reduce side effects, as well as enhance outcomes for patients in cancer therapy. This review aims to objectively evaluate the transformation of cancer treatment, emphasizing the shift towards a more precise methodology.

Background: Actinidin is an anionic thiol-proteinase predominant and unique to Chinese gooseberry or kiwifruit, whose strong digestibility enables proteins or enzymes vulnerable to digestion. The arrangement of active cysteine–thiol residues (Cys22-Cys65, Cys56-Cys98, and Cys156-Cys206) stabilizes the catalytic unit, thus allowing an effective Inhibition of α-amylase protein on exposure to the highest concentrations of actinidin under optimum conditions. When starch-rich foods are consumed with kiwifruit, starch digestion may be slowed by the inactivation of α-amylase (digestive enzyme), specifically reducing the blood sugar levels by hindering starch digestion that is helpful in diabetes mellitus. Thus, the study aimed at actinidin purification, optimization for maximal activity, and its demonstration as a potential to degrade α-amylase. Results: Protease showed a molecular mass of 27 kDa on SDS-PAGE analysis. One factor at a time method was applied for process optimization, increasing the actinidin yield up to 176.03 U/mg. The enzyme was stable at a wide pH range; however, it was most active and stable at pH 7.5. The enzyme possessed half‐life at 35 °C of 5.5 h, at 40 °C of 4.5 h, at 45 °C of 2.5 h, and at 50 °C of 1 h. Lineweaver–Burk plot showed Michaelis–Menten constant (Km: 3.14 mg/ml) and maximal velocity (Vmax: 1.428 mmol/ml/min) using casein. The actinidin activity was enhanced with Ca²⁺ while it was inhibited by Cd²⁺ and Hg²⁺ ions. The α-amylase protein was successfully inactivated upon incubation with actinidin for 30 min; around ~ 85% of the α-amylase activity diminished. IC₅₀ for inhibition of α-amylase was 2.54 mg/ml for crude actinidin and 1.86 mg/ml for purified actinidin. Conclusions: Purified Actinidin showed a 1.28-fold increase in proteolytic activity. The proteinase showed an active pH range of 3.5–8.5 under varied buffer conditions and thermostability up to 50 °C. The results revealed a significant potential utility of actinidin to retard amylase as it effectively degraded the amylolytic enzyme under in vitro conditions and could be beneficial for lowering glycemic response to ingested starch. However, further in vitro as well as in vivo studies need to be conducted under gastrointestinal conditions to establish the hypothesis.