2results about How to "Excellent thermal stability" patented technology

This invention discloses a three-dimensional integrated packaging structure and fabrication method of a glass core TGV panel with embedded heterogeneous chips. The upper and lower redistribution layers of the glass core are vertically interconnected through several metal vias. The glass core layer is provided with dry cavities, and several electronic components are embedded in the glass core layer along the Z-axis through these cavities. The electronic components are horizontally wired and transmit signals through the upper and lower redistribution layers, and are electrically connected to external circuits through the upper and lower redistribution layers and metal vias. This invention integrates the cost advantages of large-size glass panels, the performance advantages of glass materials, the vertical interconnection advantages of TGV, the density advantages of embedded packaging, and thermal management technology. It addresses the shortcomings of current packaging technologies in terms of high performance, high integration, low cost, and excellent heat dissipation, providing a system-level packaging solution with superior overall performance. This solution can improve system performance, heat dissipation performance, and integration, while reducing costs.

The application belongs to the technical field of enzyme engineering, and particularly relates to a beta-1,3-glycosyltransferase mutant and application thereof in catalyzing synthesis of rebaudioside M. The beta-1,3-glycosyltransferase mutant is obtained by mutating the beta-1,3-glycosyltransferase with an amino acid sequence shown in SEQ ID NO. 1 by at least one mutation, i.e. mutating isoleucine at the 14th position into alanine; and / or mutating asparagine at the 50th position into alanine; and / or mutating isoleucine at the 92nd position into leucine; and / or mutating leucine at the 141st position into cysteine or isoleucine. The mutant is applied to catalyzing synthesis of rebaudioside M, and is significantly superior to the wild-type enzyme in catalytic efficiency and thermal stability.